The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Reduced expression of the murine p85α subunit of phosphoinositide 3-kinase improves insulin signaling and ameliorates diabetes
Open accessAbstract
A critical component of insulin action is the enzyme phosphoinositide (PI) 3-kinase.The major regulatory subunits of PI 3-kinase, p85α and its splice variants, are encoded by the Pik3r1 gene.Heterozygous disruption of Pik3r1 improves insulin signaling and glucose homeostasis in normal mice and mice made insulin-resistant by heterozygous deletion of the Insulin receptor and/or insulin receptor substrate-1 (IRS1) genes.Reduced expression of p85 modulates the molecular balance between this protein, the p110 catalytic subunit of PI 3-kinase, and the IRS proteins.Thus, despite the decrease in p85α, PI 3-kinase activation is normal, insulin-stimulated Akt activity is increased, and glucose tolerance and insulin sensitivity are improved.Furthermore, Pik3r1 heterozygosity protects mice with genetic insulin resistance from developing diabetes.These data suggest that regulation of p85α levels may provide a novel therapeutic target for the treatment of type 2 diabetes.
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
“reduced p85α expression improves glucose homeostasis and insulin signalling in normal and insulin-resistant mice [46,47].”
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
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Role of Fatty Acids in the Pathogenesis of Insulin Resistance and NIDDM
Boden, G. (1997) · Diabetes · doi:10.2337/diab.46.1.3 · Cited by 1,728
Michael, M. D., Kulkarni, R. N., Postic, C., Previs, S. F., Shulman, G. I., Magnuson, M. A., & Kahn, C. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00015-8 · Cited by 1,296
Self-citationBrüning, J. C., Michael, M. D., Winnay, J. N., Hayashi, T., Hörsch, D., Accili, D., Goodyear, L. J., & Kahn, C. R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80155-0 · Cited by 1,173
Self-citationProtein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation
Coffer, P. J., Jin, J., & Woodgett, J. R. (1998) · Biochemical Journal · doi:10.1042/bj3350001 · Cited by 1,064
Cheatham, B., Vlahos, C. J., Cheatham, L. A., Wang, L., Blenis, J., & Kahn, C. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4902-4911.1994 · Cited by 1,062
Self-citationLeptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy
Shimomura, I., Hammer, R. E., Ikemoto, S., Brown, M. S., & Goldstein, J. L. (1999) · Nature · doi:10.1038/43448 · Cited by 1,038
The Role of Phosphoinositide 3-Kinase Lipid Products in Cell Function
Rameh, L. E., & Cantley, L. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8347 · Cited by 989
Self-citationPhosphoinositide 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
Research works printed but not linked: 1
- Cheatham, 1994, Mol Cell Biol, 14, 4902, 10.1128/MCB.14.7.4902 · DOI
Cited by
Sorted by citations
Items 101–200 of 204
A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes
Du, Z., & Uversky, V. N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102010 · Cited by 47
Molero, J. C., Waring, S. G., Cooper, A., Turner, N. A., Laybutt, D. R., Cooney, G. J., & James, D. E. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-0312 · Cited by 45
Cariou, B., Postic, C., Boudou, P., Burcelin, R., Kahn, C. R., Girard, J. R., Burnol, A., & Mauvais‐Jarvis, F. (2003) · Endocrinology · doi:10.1210/en.2003-0882 · Cited by 46
Self-citationGomez, C. L., Santiago‐Fernández, C., García‐Serrano, S., García‐Escobar, E., Gutiérrez‐Repiso, C., Rodriguez, C., Ho‐Plagaro, A., Martín‐Reyes, F., Garrido‐Sánchez, L., Valdés, S., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082615 · Cited by 48
Huo, J. S., McEachin, R. C., Cui, T. X., Duggal, N. K., Hai, T., States, D. J., & Schwartz, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508492200 · Cited by 44
McCurdy, C. E., Davidson, R. T., & Cartee, G. D. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00566.2004 · Cited by 43
Sheikh, S. E., Jan Domin, Y., Tomtitchong, P., Abel, P. D., Stamp, G., & Lalani, E. (2003) · BMC Clinical Pathology · doi:10.1186/1472-6890-3-4 · Cited by 42
Phosphoinositide 3-kinase signaling in the vertebrate retina
Rajala, R. (2010) · Journal of Lipid Research · doi:10.1194/jlr.r000232 · Cited by 46
Sbraccia, P., D’Adamo, M., & Guglielmi, V. (2021) · Eating and Weight Disorders - Studies on Anorexia Bulimia and Obesity · doi:10.1007/s40519-021-01109-4 · Cited by 43
Lee, J. S., Hmama, Z., Mui, A., & Reiner, N. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310638200 · Cited by 41
Hallmann, D., Trümper, K., Trusheim, H., Ueki, K., Kahn, C. R., Cantley, L. C., Fruman, D. A., & Hörsch, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208451200 · Cited by 41
Self-citationChapter 6 Crosstalk Between Growth Hormone and Insulin Signaling
Xu, J., & Messina, J. L. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00606-7 · Cited by 40
p85α Acts as a Novel Signal Transducer for Mediation of Cellular Apoptotic Response to UV Radiation
Song, L., Li, J., Ye, J., Yu, G., Ding, J., Zhang, D., Ouyang, W., Dong, Z., Kim, S. O., & Huang, C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00657-06 · Cited by 41
Lee, J. S., Nauseef, W. M., Moeenrezakhanlou, A., Sly, L. M., Noubir, S., Leidal, K. G., Schlomann, J. M., Krystal, G., & Reiner, N. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0906564 · Cited by 42
Blockade of IRS1 in isolated rat pancreatic islets improves glucose‐induced insulin secretion
ARAUJO, E. P. D., do Amaral, M. E. C., de Souza, C. T., Bordin, S. A., Ferreira, F., Saad, M. J. A., Boschero, A. C., Magalhães, E. C., & Velloso, L. A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03580-9 · Cited by 38
PTEN Regulation, a Novel Function for the p85 Subunit of Phosphoinositide 3-Kinase
Barber, D., Alvarado-Kristensson, M., Gonzalez-García, A., Pulido, R., & Carrera, A. (2006) · Science's STKE · doi:10.1126/stke.3622006pe49 · Cited by 43
Nicholas, L. M., Morrison, J. L., Rattanatray, L., Ozanne, S. E., Kleemann, D. O., Walker, S. K., MacLaughlin, S. M., Zhang, S., Martin‐Gronert, M. S., & McMillen, I. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084594 · Cited by 37
Use of mouse models in studying type 2 diabetes mellitus
Lee, A., & Cox, R. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399410001729 · Cited by 37
Kwok, A., Zvetkova, I., Virtue, S., Luijten, I. H. N., Huang‐Doran, I., Tomlinson, P. R., Bulger, D. A., West, J. A., Murfitt, S. A., Griffin, J. L., et al. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101020 · Cited by 36
Multiple Phosphatidylinositol 3-Kinases Regulate Vaccinia Virus Morphogenesis
McNulty, S., Bornmann, W. G., Schriewer, J. M., Werner, C., Smith, S. K., Olson, V. A., Damon, I. K., Buller, R. M. L., Heuser, J., & Kalman, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010884 · Cited by 36
Coffey, J. C., Wang, J. H., Smith, M. J. F., Laing, A. J., Bouchier‐Hayes, D. M., Cotter, T. G., & Redmond, H. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414696200 · Cited by 36
Cornier, M.-A., Bessesen, D. H., Gurevich, I., Leitner, J. W., & Draznin, B. (2006) · Diabetologia · doi:10.1007/s00125-006-0148-0 · Cited by 35
Kinoshita, H., Matsuda, N., Kaba, H., Hatakeyama, N., Azma, T., Nakahata, K., Kuroda, Y., Tange, K., Iranami, H., & Hatano, Y. (2008) · Hypertension · doi:10.1161/hypertensionaha.108.118216 · Cited by 33
Central effects of humanin on hepatic triglyceride secretion
Gong, Z., Su, K., Cui, L., Tas, E., Zhang, T., Dong, H. H., Yakar, S., & Muzumdar, R. H. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00043.2015 · Cited by 34
Argentino, D. P., Dominici, F. P., Muñoz, M. C., Al-Regaiey, K., Bartke, A., & Turyn, D. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.09.005 · Cited by 33
Characterization of the Met326Ile variant of phosphatidylinositol 3-kinase p85α
Almind, K., Delahaye, L., Hansen, T. F., OBBERGHEN, E. V., Pedersen, O. B., & Kahn, C. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042688799 · Cited by 33
Self-citationFruman, D. A. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00132-7 · Cited by 36
Self-citationGao, L., Tang, H. Y., Zeng, Q., Tang, T. S., Chen, M., & Pu, P. (2020) · Obesity Research & Clinical Practice · doi:10.1016/j.orcp.2020.06.005 · Cited by 33
Gene-targeting reveals physiological roles and complex regulation of the phosphoinositide 3-kinases
Foukas, L. C., & Okkenhaug, K. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00177-2 · Cited by 32
Gupta, I., & Gaykalova, D. A. (2024) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2024.08.004 · Cited by 31
Giacco, A., Paoli, G. D., Senese, R., Cioffi, F., Silvestri, E., Moreno, M., Ruoppolo, M., Caterino, M., Costanzo, M., Lombardi, A., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800724r · Cited by 30
Gavete, M. L., Martín, M. Á., Álvarez, C., & Escrivá, F. (2005) · Endocrinology · doi:10.1210/en.2004-1658 · Cited by 31
Huang, J., Shi, C., Gao, Y., Su, J., Shu, Y., Zeng, N., Zhai, G., Jin, X., Han, D. H., He, J., et al. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737207 · Cited by 29
Kobayashi, T., Hayashi, Y., Taguchi, K., Matsumoto, T., & Kamata, K. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01349.2005 · Cited by 29
53BP2S, Interacting with Insulin Receptor Substrates, Modulates Insulin Signaling
Hakuno, F., Kurihara, S., Watson, R. T., Pessin, J. E., & Takahashi, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702472200 · Cited by 28
Emerging Roles of BRD7 in Pathophysiology
Park, S. W., & Lee, J. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197127 · Cited by 29
In Vivo Mutagenesis of the Insulin Receptor
Okamoto, H., & Accili, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300009200 · Cited by 27
Self-citationEmbryonic vitamin D deficiency programs hematopoietic stem cells to induce type 2 diabetes
Oh, J., Riek, A. E., Bauerle, K. T., Dusso, A., McNerney, K. P., Barve, R. A., Darwech, I., Sprague, J., Moynihan, C., Zhang, R. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38849-z · Cited by 28
Insulin Resistant States and Insulin Signaling
Vollenweider, P. (2003) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2003.173 · Cited by 26
Solheim, M. H., Winnay, J. N., Batista, T. M., Molven, A., Njølstad, P. R., & Kahn, C. R. (2018) · Diabetes · doi:10.2337/db17-1509 · Cited by 24
Self-citationStunff, C. L., Dechartres, A., Mariot, V., Lotton, C., Trainor, C. D., del Giudice, E. M., Meyre, D., Bièche, I., Laurendeau, I., Froguel, P., et al. (2007) · Diabetes · doi:10.2337/db07-1273 · Cited by 25
A p85 isoform switch enhances PI3K activation on endosomes by a MAP4- and PI3P-dependent mechanism
Thapa, N., Chen, M., Cryns, V. L., & Anderson, R. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114119 · Cited by 23
Effects of Chronic Undernutrition on Glucose Uptake and Glucose Transporter Proteins in Rat Heart
Gavete, M. L., Agote, M., Martín, M. Á., Álvarez, C., & Escrivá, F. (2002) · Endocrinology · doi:10.1210/en.2002-220258 · Cited by 21
Pim3 negatively regulates glucose-stimulated insulin secretion
Vlacich, G. R., Nawijn, M. C., Webb, G. C., & Steiner, D. F. (2010) · Islets · doi:10.4161/isl.2.5.13058 · Cited by 21
Adochio, R., Leitner, J. W., Hedlund, R., & Draznin, B. (2008) · Endocrinology · doi:10.1210/en.2008-0437 · Cited by 21
Yoo, Y. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12064 · Cited by 20
Donato, N. D., Rump, A., Mirzaa, G., Alcantara, D., Oliver, A. W., Schröck, E., Dobyns, W. B., & O’Driscoll, M. (2015) · Human Mutation · doi:10.1002/humu.22933 · Cited by 19
Mendenhall, M. A., Liu, S., Portley, M. K., O’Mard, D., Fattah, R. J., Szabo, R., Bugge, T. H., Khillan, J. S., Leppla, S. H., & Moayeri, M. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0782-1 · Cited by 18
Coffey, J. C., Wang, J. H., Bouchier‐Hayes, D. M., Cotter, T. G., & Redmond, H. P. (2006) · Annals of Surgery · doi:10.1097/01.sla.0000197712.71055.12 · Cited by 18
Berthiaume, N., Carlson, C. J., Rondinone, C. M., & Zinker, B. A. (2005) · Metabolism · doi:10.1016/j.metabol.2005.05.019 · Cited by 18
The node-weighted Steiner tree approach to identify elements of cancer-related signaling pathways
Sun, Y., Ma, C., & Halgamuge, S. K. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1958-4 · Cited by 17
Kruse, M., Keyhani‐Nejad, F., Isken, F., Nitz, B., Kretschmer, A., Reischl, E., Gala, T. D. L. H., Osterhoff, M. A., Grallert, H., & Pfeiffer, A. F. H. (2015) · Diabetes · doi:10.2337/db15-0478 · Cited by 18
Divergent roles of the regulatory subunits of class IA PI3K
Kim, C., Lee, J. M., & Park, S. W. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1152579 · Cited by 16
Wang, G., Yu, Y., Cai, W., Batista, T. M., Suk, S., Noh, H. L., Hirshman, M. F., Nigro, P., Li, M. E., Softic, S., et al. (2020) · Diabetes · doi:10.2337/db20-0439 · Cited by 16
Self-citationChen, T.-C., Kuo, T., Dandan, M., Lee, R. A., Chang, M., Villivalam, S. D., Liao, S.-C., Costello, D. E., Shankaran, M., Mohammed, H., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100395 · Cited by 16
Miyake, K., Ogawa, W., Matsumoto, M., Nakamura, T., Sakaue, H., & Kasuga, M. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215880 · Cited by 15
Zhang, Y., Liu, Y., Shi, Y., Bai, C., Wang, T., Ruan, F., & Hu, C. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e32518 · Cited by 13
Molecular Mechanisms of Insulin Resistance
Draznin, B. (2019) · Contemporary Endocrinology · doi:10.1007/978-3-030-25057-7_4 · Cited by 13
Gozani, O., Field, S. J., Ferguson, C. G., Ewalt, M. D., Mahlke, C., Cantley, L. C., Prestwich, G. D., & Yuan, J. (2005) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2005.02.010 · Cited by 13
Self-citationGómez‐Hernández, A., López‐Pastor, A. R., Rubio-Longás, C., Majewski, P., Beneit, N., Viana‐Huete, V., García-Gómez, G., Fernández, S., Hribal, M. L., Sesti, G., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.10.010 · Cited by 13
Nguyen, T., Deenick, E. K., & Tangye, S. G. (2021) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2021.1945443 · Cited by 13
Protein kinase Cδ but not PKCα is involved in insulin‐induced glucose metabolism in hepatocytes
Brutman‐Barazani, T., Horovitz‐Fried, M., Aga‐Mizrachi, S., Brand, C., Brodie, C., Roša, J., & Sampson, S. R. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24078 · Cited by 12
Role of the liver in glucose homeostasis in PI 3-kinase p85α-deficient mice
Aoki, K., Matsui, J., Kubota, N., Nakajima, H., Iwamoto, K., Takamoto, I., Tsuji, Y., Ohno, A., Mori, S., Tokuyama, K., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90528.2008 · Cited by 12
Loss of PI3 kinase association improves the sensitivity of secondary mutation of KIT to Imatinib
Zhu, G., Shi, J., Zhang, S., Guo, Y., Huang, L., Zhao, H., Jiang, Y., & Sun, J. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-0377-9 · Cited by 11
Mechanisms Underlying Insulin Resistance in Human Pregnancy and Gestational Diabetes Mellitus
McCurdy, C. E., & Friedman, J. E. (2010) · Springer eBooks · doi:10.1007/978-1-84882-120-0_9 · Cited by 11
Chen, S., Yan, W., Huang, J., Ge, D., Yao, Z. J., & Gu, D. (2005) · Diabetic Medicine · doi:10.1111/j.1464-5491.2005.01490.x · Cited by 12
Osteocalcin of maternal and embryonic origins synergize to establish homeostasis in offspring
Junior, D. C. P., Delgado, I. C., Yang, H., Clemenceau, A., Corvelo, A., Narzisi, G., Musunuri, R., Berger, J. M., Hendricks, L., Tokumura, K., et al. (2024) · EMBO Reports · doi:10.1038/s44319-023-00031-3 · Cited by 15
Liangzi, F., Zheng, Q., & Han, J. (2021) · Digital Chinese Medicine · doi:10.1016/j.dcmed.2021.03.003 · Cited by 8
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
Lee, J. M., Liu, R., & Park, S. W. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab073 · Cited by 7
Old biliverdin reductase: Links to insulin resistance and may be a novel therapeutic target
Wu, B., Liu, X., & Shen, J. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2008.02.007 · Cited by 7
Diet-induced obesity obstructs insulin signaling in the heart
Young, L. H. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01088.2009 · Cited by 7
Yoshida, K., Matsuoka, T., Kobatake, Y., Takashima, S., & NISHII, N. (2022) · Journal of Veterinary Medical Science · doi:10.1292/jvms.21-0325 · Cited by 6
Baudler, S., Krone, W., & Brüning, J. C. (2003) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/s1521-690x(03)00039-3 · 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
Teixeira, L. C. R., Pereira, J. D., Mamede, I., Caramelli, P., Silva, V., Veloso, A., Luizon, M. R., & Gomes, K. B. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70196 · Cited by 4
Chen, H., Li, R., Ma, X., Qiu, Z., & Qiu, Y. (2024) · Network Modeling Analysis in Health Informatics and Bioinformatics · doi:10.1007/s13721-024-00444-7 · Cited by 5
PI3K signaling: a crossroads of metabolic regulation
Braccini, L., Ciraolo, E., Morello, F., Lu, X., & Hirsch, E. (2009) · Expert Review of Endocrinology & Metabolism · doi:10.1586/eem.09.19 · Cited by 4
Molecular Mechanisms of Insulin Resistance
Draznin, B. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-192-5_6 · Cited by 4
Toušková, V., Kloučková, J., Ďurovcová, V., Lacinová, Z., Kaválková, P., Trachta, P., Kosák, M., Mráz, M., Haluzíková, D., Hána, V., et al. (2016) · Physiological Research · doi:10.33549/physiolres.933244 · Cited by 4
MEYTS, P. D., & Lefèbvre, P. J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813814-4.00017-1 · Cited by 4
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
Self-citationLipid Research Picks Up Speed on the Slopes of Taos
Field, S. J., Lamia, K. A., Rameh, L. E., & Cantley, L. C. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00150-8 · Cited by 3
Self-citationLi, Q., Pei, J., Wang, L., Li, J., Qin, D., Mo, H., & Zhang, H. P. (2024) · Natural Product Communications · doi:10.1177/1934578x241280871 · Cited by 2
Kim, S., Cao, T., Wan, Z., Kim, J., Li, Z., Radden, L. A., Santhanam, R., Ko, E. C., Osaki, T., Spitz, S., et al. (2025) · Advanced Healthcare Materials · doi:10.1002/adhm.202502711 · Cited by 2
Zieleniak, A., Żurawska-Kliś, M., Laszcz, K., Bulash, K., Pacyga, D., Cypryk, K., Woźniak, L. A., & Wójcik, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313094 · Cited by 3
Insulin Action in the Islet β-Cell
Kulkarni, R. (2007) · Springer eBooks · doi:10.1007/978-0-387-72204-7_7 · Cited by 2
White, M. F. (2024) · Wiley eBooks · doi:10.1002/9781119697473.ch9 · Cited by 2
Modulation of insulin resistance by PUFA in metabolic tissues
Kopál, M., Muchová, J., & Ďuračková, Z. (2013) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201200229 · Cited by 1
FUJII, N. L. (2016) · Springer eBooks · doi:10.1007/978-4-431-55720-3_9 · Cited by 1
Ukil, S., Sinha, M., Varshney, L., & Agrawal, S. (2009) · Communications in computer and information science · doi:10.1007/978-3-642-03547-0_42
Insulin Resistance, Dyslipidemia, Type 2 Diabetes Mellitus and Metabolic Syndrome
Das, U. N. (2011) · Springer eBooks · doi:10.1007/978-94-007-0495-4_9
Transgenic Models of Impaired Insulin Signaling
Oriente, F., & Accili, D. (2007) · Springer eBooks · doi:10.1007/978-0-387-72204-7_9
Self-citationThe Relationship Between the Insulin Receptor Substrates and Metabolic Disease
White, M. F. (2008) · Humana Press eBooks · doi:10.1007/978-1-60327-116-5_14
(2007) · Springer eBooks · doi:10.1007/978-3-540-47818-8_25
Molecular Basis of Role of Insulin Resistance in Pathophysiology of Alzheimer’s Disease
Gupta, A. (2022) · International Journal of Health Sciences and Pharmacy · doi:10.47992/ijhsp.2581.6411.0094
Paradoxical dominant negative activity of an immunodeficiency-associated activating PIK3R1 variantPreprint
Tomlinson, P. R., Knox, R. G., Perišić, O., Su, H. C., Brierley, G. V., Williams, R. L., & Semple, R. K. (2024) · eLife · doi:10.7554/elife.94420.1
Paradoxical dominant negative activity of an immunodeficiency-associated activating PIK3R1 variantPreprint
Tomlinson, P. R., Knox, R. G., Perišić, O., Su, H. C., Brierley, G. V., Williams, R. L., & Semple, R. K. (2025) · eLife · doi:10.7554/elife.94420.2
p85β acts as a transcription cofactor and cooperates with BCLAF1 in the nucleus
Wang, P., Mak, V. C. Y., Rao, L., Wu, Q., Zhou, Y., Sharma, R., Kwon, S. C., & Cheung, L. W. T. (2025) · Nature Communications · doi:10.1038/s41467-025-56532-3
Xu, H., Huang, R., Jin, J., Wu, Y., Cheng, Z., Wang, M., Ye, X., Lai, M., & Zhang, D. D. (2026) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2026.101814
Metadata
- Authors
- Mauvais-Jarvis, F., Ueki, K., Fruman, D. A., Hirshman, M. F., Sakamoto, K., Goodyear, L. J., Iannacone, M., Accili, D., Cantley, L. C., & Kahn, C. R.
- Affiliations
- Joslin Diabetes Center (US)
- Beth Israel Deaconess Medical Center (US)
- Columbia University (US)
- Corresponding author
- Kahn, C. Ronald
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2002-01-01
- Volume
- 109
- Issue
- 1
- Pages
- 141-149
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W4243898144
- Cited by
- 207
- References
- 38
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 11 · 2023: 1 · 2022: 5 · 2021: 6 · 2020: 10 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 3 · 2015: 6 · 2014: 2 · 2013: 8 · 2012: 6
- FWCI
- 6.16
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Funders
- Damon Runyon Cancer Research Foundation
- National Institutes of Health (GM41890)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK033201)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- phosphatidylinositol 3-kinase, PIK3R1, insulin signaling, insulin resistance, type 2 diabetes, insulin receptor, IRS-1, Akt, glucose homeostasis, glucose tolerance, heterozygous knockout mice, therapeutic target
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