Increased Insulin Sensitivity and Obesity Resistance in Mice Lacking the Protein Tyrosine Phosphatase-1B Gene
Abstract
Protein tyrosine phosphatase–1B (PTP-1B) has been implicated in the negative regulation of insulin signaling. Disruption of the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP-1B +/+ littermates. The enhanced insulin sensitivity of the PTP-1B −/− mice was also evident in glucose and insulin tolerance tests. The PTP-1B −/− mice showed increased phosphorylation of the insulin receptor in liver and muscle tissue after insulin injection in comparison to PTP-1B +/+ mice. On a high-fat diet, the PTP-1B −/− and PTP-1B +/− mice were resistant to weight gain and remained insulin sensitive, whereas the PTP-1B +/+ mice rapidly gained weight and became insulin resistant. These results demonstrate that PTP-1B has a major role in modulating both insulin sensitivity and fuel metabolism, thereby establishing it as a potential therapeutic target in the treatment of type 2 diabetes and obesity.
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PTP1B inhibits leptin and insulin signaling in cultured cells and in vivo via dephosphorylation of Jak2.
“the protein tyrosine phosphatase (PTP)1B inhibits leptin and insulin signaling in cultured cells and in vivo via dephosphorylation of Jak2 (48, 93).”
From Leptin and the Central Nervous System Control of Glucose Metabolism (2011) · cites this paper as [48]
Cites
Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
Li, E., Bestor, T. H., & Jaenisch, R. (1992) · Cell · doi:10.1016/0092-8674(92)90611-f · Cited by 3,984 · see citing works
Protection from obesity-induced insulin resistance in mice lacking TNF-α function
Uysal, K. T., Wiesbrock, S. M., Marino, M. W., & Hotamisligil, G. S. (1997) · Nature · doi:10.1038/39335 · Cited by 2,234 · see citing works
White, M. F., & Kahn, C. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42297-6 · Cited by 1,723 · see citing works
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 · see citing works
Mechanism of Inhibition of Protein-tyrosine Phosphatases by Vanadate and Pervanadate
Huyer, G., Liu, S., Kelly, J., Moffat, J., Payette, P., Kennedy, B. P., Tsaprailis, G., Gresser, M. J., & Ramachandran, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.843 · Cited by 815 · see citing works
Self-citationYou-Ten, K. E., Muise, E. S., Itié, A., Michaliszyn, E., Wagner, J., Jothy, S., Lapp, W. S., & Tremblay, M. L. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.5.683 · Cited by 361 · see citing works
Self-citationProtein Tyrosine Phosphatase 1B Interacts With the Activated Insulin Receptor
Seely, B. L., Staubs, P. A., Reichart, D. R., Berhanu, P., Milarski, K. L., Saltiel, A. R., Kusari, J., & Olefsky, J. M. (1996) · Diabetes · doi:10.2337/diab.45.10.1379 · Cited by 319 · see citing works
Bandyopadhyay, D., Kusari, A. B., Kenner, K. A., Liu, F., Chernoff, J., Gustafson, T. A., & Kusari, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1639 · Cited by 258 · see citing works
Insulin action impaired by deficiency of the G-protein subunit Giα2
Moxham, C. M., & Malbon, C. C. (1996) · Nature · doi:10.1038/379840a0 · Cited by 214 · see citing works
Rothenberg, P., Lane, W. S., Karasik, A., Backer, J., White, M. F., & Kahn, C. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92976-5 · Cited by 196 · see citing works
Microinjection of a protein-tyrosine-phosphatase inhibits insulin action in Xenopus oocytes.
Cicirelli, M. F., Tonks, N. K., Diltz, C. D., Weiel, J. E., Fischer, E. H., & Krebs, E. G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5514 · Cited by 152 · see citing works
Selective Down-regulation of the Insulin Receptor Signal by Protein-tyrosine Phosphatases α and ∊
M⊘ller, N. P. H., M⊘ller, K. B., Lammers, R., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.23126 · Cited by 147 · see citing works
Schaapveld, R. Q. J., Schepens, J. T. G., Robinson, G. W., Attema, J., Oerlemans, F. T. J. J., Fransen, J. A. M., Streuli, M., Wieringa, B., Hennighausen, L. G., & Hendriks, W. J. A. J. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8630 · Cited by 127 · see citing works
Ren, J., Li, P.-M., Zhang, W. R., Sweet, L. J., Cline, G. W., Shulman, G. I., Livingston, J. N., & Goldstein, B. J. (1998) · Diabetes · doi:10.2337/diabetes.47.3.493 · Cited by 117 · see citing works
LMW-PTP Is a Negative Regulator of Insulin-Mediated Mitotic and Metabolic Signalling
Chiarugi, P., Cirri, P., Marra, F., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7355 · Cited by 104 · see citing works
Maegawa, H., Ide, R., Hasegawa, M., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7724 · Cited by 87 · see citing works
Expression of protein‐tyrosine phosphatases in the major insulin target tissues
Norris, K. E., Norris, F., Kono, D. H., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01133-2 · Cited by 62 · see citing works
Khandelwal, R. L., & Pugazhenthi, S. (1995) · Molecular and Cellular Biochemistry · doi:10.1007/bf01075922 · Cited by 44 · see citing works
Jacob, K. K., Sap, J., & Stanley, F. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.8.4800 · Cited by 39 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Insulin signalling and the regulation of glucose and lipid metabolism
Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326 · see citing works
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 · see citing works
Protein Tyrosine Phosphatases in the Human Genome
Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886 · see citing works
Glucose Transporters and Insulin Action — Implications for Insulin Resistance and Diabetes Mellitus
Shepherd, P. R., & Kahn, B. B. (1999) · New England Journal of Medicine · doi:10.1056/nejm199907223410406 · Cited by 1,295 · see citing works
Klaman, L. D., Boss, O., Peroni, O. D., Kim, J. K., Martino, J. L., Zabolotny, J. M., Moghal, N., Lubkin, M., Kim, Y.-B., Sharpe, A. H., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5479-5489.2000 · Cited by 1,235 · see citing works
The Human Obesity Gene Map: The 2005 Update
Rankinen, T., Zuberi, A., Chagnon, Y. C., Weisnagel, S. J., Argyropoulos, G., Walts, B., Pérusse, L., & Bouchard, C. (2006) · Obesity · doi:10.1038/oby.2006.71 · Cited by 1,119 · see citing works
Insulin resistance: review of the underlying molecular mechanisms
Yaribeygi, H., Farrokhi, F. R., Butler, A. E., & Sahebkar, A. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.27603 · Cited by 929 · see citing works
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works
Signaling pathways in insulin action: molecular targets of insulin resistance
Pessin, J. E., & Saltiel, A. R. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10582 · Cited by 939 · see citing works
Cellular Mechanisms for Insulin Resistance in Normal Pregnancy and Gestational Diabetes
Barbour, L. A., McCurdy, C. E., Hernandez, T. L., Kirwan, J. P., Catalano, P. M., & Friedman, J. E. (2007) · Diabetes Care · doi:10.2337/dc07-s202 · Cited by 811 · see citing works
SIRT1 Improves Insulin Sensitivity under Insulin-Resistant Conditions by Repressing PTP1B
Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.014 · Cited by 766 · see citing works
Biochemical and cellular properties of insulin receptor signalling
Haeusler, R. A., McGraw, T. E., & Accili, D. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.89 · Cited by 739 · see citing works
Prevention of fat-induced insulin resistance by salicylate
Kim, J. K., Kim, Y.-J., Fillmore, J. J., Chen, Y., Moore, I., Lee, J., Yuan, M., Li, Z. W., Karin, M., Perret, P., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11559 · Cited by 737 · see citing works
Mori, H., Hanada, R., Hanada, T., Aki, D., Mashima, R., Nishinakamura, H., Torisu, T., Chien, K. R., Yasukawa, H., & Yoshimura, A. (2004) · Nature Medicine · doi:10.1038/nm1071 · Cited by 651 · see citing works
Neuronal PTP1B regulates body weight, adiposity and leptin action
Bence, K. K., Delibegovic, M., Xue, B., Gorgun, C. Z., Hotamisligil, G. S., Neel, B. G., & Kahn, B. B. (2006) · Nature Medicine · doi:10.1038/nm1435 · Cited by 633 · see citing works
Reactive oxygen species enhance insulin sensitivity
Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.009 · Cited by 581 · see citing works
The contribution of bone to whole-organism physiology
Karsenty, G., & Ferron, M. (2012) · Nature · doi:10.1038/nature10763 · Cited by 537 · see citing works
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542 · see citing works
Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase
McClung, J. P., Roneker, C. A., Mu, W., Lisk, D. J., Langlais, P., Liu, F., & Lei, X. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308096101 · Cited by 536 · see citing works
Leptin, Obesity, and Leptin Resistance: Where Are We 25 Years Later
Izquierdo, A. G., Crujeiras, A. B., Casanueva, F. F., & Carreira, M. C. (2019) · Nutrients · doi:10.3390/nu11112704 · Cited by 525 · see citing works
Mahadev, K., Zilbering, A., Zhu, L., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100109200 · Cited by 509 · see citing works
Howard, J. K., Cave, B. J., Oksanen, L. J., Tzameli, I., Bjørbæk, C., & Flier, J. S. (2004) · Nature Medicine · doi:10.1038/nm1072 · Cited by 490 · see citing works
Koerner, A., Kratzsch, J., & Kiess, W. (2005) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2005.07.008 · Cited by 471 · see citing works
Current views on type 2 diabetes
Lin, Y., & Sun, Z. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0260 · Cited by 457 · see citing works
Insulin signaling in health and disease
Saltiel, A. R. (2021) · Journal of Clinical Investigation · doi:10.1172/jci142241 · Cited by 446 · see citing works
Stiles, B., Wang, Y., Stahl, A., Bassilian, S., Lee, W. P., Kim, Y.-J., Sherwin, R., Devaskar, S., Lesche, R., Magnuson, M. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308617100 · Cited by 436 · see citing works
Medicinal strategies in the treatment of obesity
Bray, G. A., & Tartaglia, L. A. (2000) · Nature · doi:10.1038/35007544 · Cited by 432 · see citing works
Protein-tyrosine phosphatase 1B expression is induced by inflammation in vivo.
Zabolotny, J. M., Kim, Y.-B., Welsh, L. A., Kershaw, E. E., Neel, B. G., & Kahn, B. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800061200 · Cited by 404 · see citing works
Thiol-based redox switches in eukaryotic proteins
Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works
Leptin and the Central Nervous System Control of Glucose Metabolism
Morton, G. J., & Schwartz, M. W. (2011) · Physiological Reviews · doi:10.1152/physrev.00007.2010 · Cited by 338 · see citing works
“Similar to SOCS-3, protein tyrosine phosphatase (PTP) 1B may also inhibit LepRb signaling via dephosphorylation of Jak2.”
BackgroundInfluentialAndrogens alter T-cell immunity by inhibiting T-helper 1 differentiation
Kissick, H. T., Sanda, M. G., Dunn, L. K., Pellegrini, K. L., On, S. T., Noel, J. K., & Arredouani, M. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402468111 · Cited by 337 · see citing works
The role of mammalian target of rapamycin (mTOR) in insulin signaling
Yoon, M.-S. (2017) · Nutrients · doi:10.3390/nu9111176 · Cited by 300 · see citing works
Skeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282 · see citing works
Mechanism of increased risk of insulin resistance in aging skeletal muscle
Shou, J., Chen, P.-J., & Xiao, W.-H. (2020) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-020-0523-x · Cited by 283 · see citing works
S-Nitrosation of the Insulin Receptor, Insulin Receptor Substrate 1, and Protein Kinase B/Akt
Carvalho-Filho, M. A., Ueno, M., Hirabara, S. M., Seabra, A. B., Carvalheira, J. B. C., de Oliveira, M. G., Velloso, L. A., Curi, R., & Saad, M. J. A. (2005) · Diabetes · doi:10.2337/diabetes.54.4.959 · Cited by 277 · see citing works
The adipocyte as an active participant in energy balance and metabolism
Badman, M. K., & Flier, J. S. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.058 · Cited by 256 · see citing works
Role of insulin-induced reactive oxygen species in the insulin signaling pathway
Goldstein, B. J., Mahadev, K., Wu, X., Zhu, L., & Motoshima, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1021 · Cited by 238 · see citing works
Bioactive compounds from marine macroalgae and their hypoglycemic benefits
Zhao, C., Yang, C., Liu, B., Lin, L., Sarker, S. D., Nahar, L., Yu, H., Cao, H., & Xiao, J. (2018) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2017.12.001 · Cited by 235 · see citing works
Schéle, E., Grahnemo, L., Anesten, F., Hallén, A., Bäckhed, F., & Jansson, J.-O. (2013) · Endocrinology · doi:10.1210/en.2012-2151 · Cited by 209 · see citing works
Mechanisms of Hepatic Very Low-Density Lipoprotein Overproduction in Insulin Resistance
Adeli, K., Taghibiglou, C., Van Iderstine, S. C., & Lewis, G. F. (2001) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(01)00084-6 · Cited by 194 · see citing works
Diet-induced obesity leads to the development of leptin resistance in vagal afferent neurons
de Lartigue, G., Barbier de la Serre, C., Espero, E., Lee, J., & Raybould, H. E. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00056.2011 · Cited by 179 · see citing works
Reed, A. S., Unger, E. K., Olofsson, L. E., Piper, M. L., Myers, M. G., & Xu, A. W. (2010) · Diabetes · doi:10.2337/db09-1024 · Cited by 176 · see citing works
Time-Resolved and Tissue-Specific Systems Analysis of the Pathogenesis of Insulin Resistance
Kleemann, R., van Erk, M., Verschuren, L., van den Hoek, A. M., Koek, M., Wielinga, P. Y., Jie, A., Pellis, L., Bobeldijk-Pastorova, I., Kelder, T., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008817 · Cited by 146 · see citing works
Smith, F. M., Holt, L. J., Garfield, A. S., Charalambous, M., Koumanov, F., Perry, M., Bazzani, R., Sheardown, S. A., Hegarty, B. D., Lyons, R. J., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02087-06 · Cited by 134 · see citing works
Forkhead Box O as a Sensor, Mediator, and Regulator of Redox Signaling
de Keizer, P. L. J., Burgering, B. M. T., & Dansen, T. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3403 · Cited by 131 · see citing works
Zinc ions modulate protein tyrosine phosphatase 1B activity
Bellomo, E., Massarotti, A., Hogstrand, C., & Maret, W. (2014) · Metallomics · doi:10.1039/c4mt00086b · Cited by 108 · see citing works
Increased Hypothalamic Protein Tyrosine Phosphatase 1B Contributes to Leptin Resistance with Age
Morrison, C. D., White, C. L., Wang, Z., Lee, S.-Y., Lawrence, D. S., Cefalu, W. T., Zhang, Z.-Y., & Gettys, T. W. (2007) · Endocrinology · doi:10.1210/en.2006-0672 · Cited by 106 · see citing works
Impact of Leptin-Mediated Sympatho-Activation on Cardiovascular Function in Obese Mice
Belin de Chantemèle, E. J., Mintz, J. D., Rainey, W. E., & Stepp, D. W. (2011) · Hypertension · doi:10.1161/hypertensionaha.110.168427 · Cited by 103 · see citing works
Pauli, J. R., Ropelle, E. R., Cintra, D. E., Carvalho‐Filho, M. A., Moraes, J. C., De Souza, C. T., Velloso, L. A., Carvalheira, J. B. C., & Saad, M. J. A. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.142414 · Cited by 97 · see citing works
Schwartz, M. W., & Niswender, K. D. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0906 · Cited by 93 · see citing works
Turdi, S., Ge, W., Hu, N., Bradley, K. M., Wang, X., & Ren, J. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.12.007 · Cited by 88 · see citing works
Carvalho-Filho, M. A., Ueno, M., Carvalheira, J. B. C., Velloso, L. A., & Saad, M. J. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00422.2005 · Cited by 84 · see citing works
M<scp>ETABOLIC</scp> L<scp>ESSONS FROM</scp> G<scp>ENETICALLY</scp> L<scp>EAN</scp> M<scp>ICE</scp>
Reitman, M. L. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.010402.102849 · Cited by 75 · see citing works
Development of Diabesity in Mice with Neuronal Deletion of Shp2 Tyrosine Phosphatase
Krajewska, M., Banares, S., Zhang, E. E., Huang, X., Scadeng, M., Jhala, U. S., Feng, G.-S., & Krajewski, S. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070594 · Cited by 72 · see citing works
Belin de Chantemèle, E. J., Muta, K., Mintz, J., Tremblay, M. L., Marrero, M. B., Fulton, D. J., & Stepp, D. W. (2009) · Circulation · doi:10.1161/circulationaha.109.853077 · Cited by 67 · see citing works
Self-citationModulation of glucose transport in skeletal muscle by reactive oxygen species
Katz, A. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01066.2006 · Cited by 65 · see citing works
Ferhati, X., Matassini, C., Fabbrini, M. G., Goti, A., Morrone, A., Cardona, F., Moreno-Vargas, A. J., & Paoli, P. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.03.053 · Cited by 53 · see citing works
Atkinson, T. J. (2008) · Obesity Reviews · doi:10.1111/j.1467-789x.2007.00412.x · Cited by 49 · see citing works
Balland, E., Chen, W., Dodd, G. T., Conductier, G., Coppari, R., Tiganis, T., & Cowley, M. A. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.061 · Cited by 44 · see citing works
de Chantemèle, E. J. B., Ali, M. I., Mintz, J. D., Rainey, W. E., Tremblay, M. L., Fulton, D. J., & Stepp, D. W. (2012) · Hypertension · doi:10.1161/hypertensionaha.112.196295 · Cited by 25 · see citing works
Self-citationGarcía-Ruiz, I., Solís-Muñoz, P., Gómez-Izquierdo, É., Muñoz-Yagüe, M. T., Valverde, Á. M., & Solís-Herruzo, J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342709 · Cited by 22 · see citing works
Yamanishi, K., Hashimoto, T., Miyauchi, M., Mukai, K., Ikubo, K., Uwa, N., Watanabe, Y., Ikawa, T., Okuzaki, D., Okamura, H., et al. (2019) · Biomedical Reports · doi:10.3892/br.2019.1259 · Cited by 13 · see citing works
- Authors
- Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., Ramachandran, C., Gresser, M. J., Tremblay, M. L., & Kennedy, B. P.
- Affiliations
- McGill University (CA)
- Merck Canada Inc. (Canada) (CA)
- Department of Biochemistry, McGill University, 3655 Drummond Street, Montreal, Quebec, Canada, H3G 1Y6.
- Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada, K1H 8M5.
- Corresponding author
- Kennedy, Brian P.
- Venue
- Science
- Published
- 1999-03-05
- Volume
- 283
- Issue
- 5407
- Pages
- 1544-1548
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2123229219
- Cited by
- 2,210
- References
- 19
- Citations by year
- 2026: 36 · 2025: 32 · 2024: 49 · 2023: 51 · 2022: 41 · 2021: 56 · 2020: 60 · 2019: 64 · 2018: 62 · 2017: 87 · 2016: 84 · 2015: 91 · 2014: 99 · 2013: 112 · 2012: 133
- FWCI
- 28.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- PTP1B, insulin sensitivity, insulin resistance, obesity, insulin signaling, insulin receptor phosphorylation, glucose tolerance, high-fat diet, type 2 diabetes, knockout mice, fuel metabolism
- MeSH terms
- Animals, Blood Glucose, Diabetes Mellitus, Type 2, Dietary Fats, Glucose Tolerance Test, Insulin, Insulin Resistance, Liver, Male, Obesity, Phosphoproteins, Phosphorylation, Receptor, Insulin, Signal Transduction, Protein Tyrosine Phosphatases, Mice, Knockout, Gene Targeting, Muscle, Skeletal, Phosphotyrosine, Mice, Insulin Receptor Substrate Proteins
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