Cited by 953PI3K/AKT/mTOR signaling in cancerMetabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase Signaling

The DOI matches its Crossref record; 333 of the 338 references it cites were found in a registry or an index.

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

Open access

SHEPHERD, Peter R., WITHERS, Dominic J., SIDDLE, Kenneth·1998·Biochemical Journal

DOI 10.1042/bj3330471PMC PMC1219607

Open this paper in CoChat — free account Open PDF

Abstract

Insulin plays a key role in regulating a wide range of cellular processes. However, until recently little was known about the signalling pathways that are involved in linking the insulin receptor with downstream responses. It is now apparent that the activation of class 1a phosphoinositide 3-kinase (PI 3-kinase) is necessary and in some cases sufficient to elicit many of insulin's effects on glucose and lipid metabolism. The lipid products of PI 3-kinase act as both membrane anchors and allosteric regulators, serving to localize and activate downstream enzymes and their protein substrates. One of the major ways these lipid products of PI 3-kinase act in insulin signalling is by binding to pleckstrin homology (PH) domains of phosphoinositide-dependent protein kinase (PDK) and protein kinase B (PKB) and in the process regulating the phosphorylation of PKB by PDK. Using mechanisms such as this, PI 3-kinase is able to act as a molecular switch to regulate the activity of serine/threonine-specific kinase cascades important in mediating insulin's effects on endpoint responses.

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

Crossref · 10.1042/bj3330471

Cites

333 of 333 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689
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
A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002).
Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248
Mechanism of activation of protein kinase B by insulin and IGF‐1.
Alessi, D. R., Andjelković, M., Caudwell, B., Cron, P. D., MORRICE, N. A., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,014
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 2,874
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
SH2 domains recognize specific phosphopeptide sequences
Songyang, Z. (1993) · Cell · doi:10.1016/0092-8674(93)90404-e · Cited by 2,620
Regulation of neuronal survival by the serine-threonine protein kinase Akt
Dudek, H., Datta, S. R., Franke, T. F., Birnbaum, M. J., Yao, R., Cooper, G. M., Segal, R. A., Kaplan, D. R., & Greenberg, M. E. (1997) · Science · doi:10.1126/science.275.5300.661 · Cited by 2,436
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
Burgering, B. M. T., & Coffer, P. J. (1995) · Nature · doi:10.1038/376599a0 · Cited by 2,076
The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
Franke, T. F., Yang, S., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., & Tsichlis, P. N. (1995) · Cell · doi:10.1016/0092-8674(95)90534-0 · Cited by 2,001
Phosphatidylinositol-3-OH kinase direct target of Ras
Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954
Disruption of IRS-2 causes type 2 diabetes in mice
Withers, D. J., Gutierrez, J. S., Towery, H. H., Burks, D. J., Ren, J., Previs, S. F., Zhang, Y., Bernal, D., Pons, S., Shulman, G. I., et al. (1998) · Nature · doi:10.1038/36116 · Cited by 1,775
Self-citation
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Gutkind, J. S. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,629
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
Direct Regulation of the Akt Proto-Oncogene Product by Phosphatidylinositol-3,4-bisphosphate
Franke, T. F., Kaplan, D. R., Cantley, L. C., & Toker, A. (1997) · Science · doi:10.1126/science.275.5300.665 · Cited by 1,462
Requirement for Phosphatidylinositol-3 Kinase in the Prevention of Apoptosis by Nerve Growth Factor
Yao, R., & Cooper, G. M. (1995) · Science · doi:10.1126/science.7701324 · Cited by 1,393
Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
Muslin, A. J., Tanner, J. W., Allen, P. M., & Shaw, A. S. (1996) · Cell · doi:10.1016/s0092-8674(00)81067-3 · Cited by 1,385
Signalling through the lipid products of phosphoinositide-3-OH kinase
Toker, A., & Cantley, L. C. (1997) · Nature · doi:10.1038/42648 · Cited by 1,306
Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation
Kohn, A. D., Summers, S. A., Birnbaum, M. J., & Roth, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31372 · Cited by 1,284
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
Dual Role of Phosphatidylinositol-3,4,5-trisphosphate in the Activation of Protein Kinase B
Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R. J., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F. P., & Hawkins, P. T. (1997) · Science · doi:10.1126/science.277.5325.567 · Cited by 1,216
FUNCTION AND REGULATION OF RAS
Lowy, D. R., & Willumsen, B. M. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004223 · Cited by 1,164
Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB
Kauffmann-Zeh, A., Rodriguez‐Viciana, P., Ulrich, E., Gilbert, C. S., Coffer, P. J., Downward, J., & Evan, G. I. (1997) · Nature · doi:10.1038/385544a0 · Cited by 1,144
Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
Arcaro, A., & Wymann, M. P. (1993) · Biochemical Journal · doi:10.1042/bj2960297 · Cited by 1,138
RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1
Burnett, P. E., Barrow, R. K., Cohen, N. A., Snyder, S. H., & Sabatini, D. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1432 · Cited by 1,130
Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1
Tamemoto, H., Kadowaki, T., Tobe, K., Yagi, T., Sakura, H., Hayakawa, T., Terauchi, Y., Ueki, K., Kaburagi, Y., Satoh, S., et al. (1994) · Nature · doi:10.1038/372182a0 · Cited by 1,081
The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal.Preprint
Kennedy, S. G., Wagner, A. J., Conzen, S. D., Jordán, J., Bellacosa, A., Tsichlis, P. N., & Hay, N. (1997) · Genes & Development · doi:10.1101/gad.11.6.701 · Cited by 1,076
Phosphatidylinositol 3-Kinase Activation Is Required for Insulin Stimulation of pp70 S6 Kinase, DNA Synthesis, and Glucose Transporter Translocation
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
Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B
Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061
Role of Phosphoinositide 3-OH Kinase in Cell Transformation and Control of the Actin Cytoskeleton by Ras
Rodriguez‐Viciana, P., Warne, P. H., Khwaja, A., Marte, B. M., Pappin, D., Das, P., Waterfield, M. D., Ridley, A. J., & Downward, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80226-3 · Cited by 1,060
Role of Translocation in the Activation and Function of Protein Kinase B
Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31515 · Cited by 1,051
Matrix adhesion and Ras transformation both activate a phosphoinositide 3‐OH kinase and protein kinase B/Akt cellular survival pathway
Khwaja, A., Rodriguez‐Viciana, P., Wennström, S., Warne, P. H., & Downward, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.10.2783 · Cited by 1,041
Antiapoptotic Signalling by the Insulin-Like Growth Factor I Receptor, Phosphatidylinositol 3-Kinase, and Akt
Kulik, G., Klippel, A., & Weber, M. J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1595 · Cited by 1,038
Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
Whitman, M., Downes, C. P., Keeler, M. L., Keller, T. L., & Cantley, L. C. (1988) · Nature · doi:10.1038/332644a0 · Cited by 1,018
Structural basis for the binding of proline-rich peptides to SH3 domains
Yu, H., Chen, J., Feng, S., Dalgarno, D. C., Brauer, A. W., & Schrelber, S. L. (1994) · Cell · doi:10.1016/0092-8674(94)90367-0 · Cited by 1,003
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
Phosphoinositide 3-kinases: A conserved family of signal transducers
Vanhaesebroeck, B., Leevers, S. J., Panayotou, G., & Waterfield, M. D. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01061-x · Cited by 961
Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate.
Nakanishi, H., Brewer, K., & Exton, J. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54107-7 · Cited by 956
Modular binding domains in signal transduction proteins
Cohen, G. B., Ren, R., & Baltimore, D. (1995) · Cell · doi:10.1016/0092-8674(95)90406-9 · Cited by 951
SH2 and SH3 domains: From structure to function
Pawson, T. J., & Gish, G. D. (1992) · Cell · doi:10.1016/0092-8674(92)90504-6 · Cited by 940
Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
Songyang, Z., Carraway, K. L., Eck, M. J., Harrison, S. C., Feldman, R. A., Mohammadi, M., Schlessinger, J., Hubbard, S. R., Smith, D. P., Eng, C., et al. (1995) · Nature · doi:10.1038/373536a0 · Cited by 919
Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. Studies with a selective inhibitor wortmannin.
Okada, T., Kawano, Y., Sakakibara, T., Hazeki, O., & Ui, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41901-6 · Cited by 911
Insulin Action and the Insulin Signaling Network*
Cheatham, B., & Kahn, C. R. (1995) · Endocrine Reviews · doi:10.1210/edrv-16-2-117 · Cited by 885
4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathwayPreprint
Gingras, A., Kennedy, S. G., O'Leary, M., Sonenberg, N., & Hay, N. (1998) · Genes & Development · doi:10.1101/gad.12.4.502 · Cited by 885
Phosphorylation of the Translational Repressor PHAS-I by the Mammalian Target of Rapamycin
Brunn, G. J., Hudson, C. C., Sekulić, A., Williams, J. M., Hosoi, H., Houghton, P. J., Lawrence, J. C., & Abraham, R. T. (1997) · Science · doi:10.1126/science.277.5322.99 · Cited by 846
Role of IRS-2 in insulin and cytokine signalling
Sun, X. J., Wang, L.-M., Zhang, Y., Yenush, L., Myers, M. G., Glasheen, E. M., Lane, W. S., Pierce, J. H., & White, M. F. (1995) · Nature · doi:10.1038/377173a0 · Cited by 842
Phosphorylation and Activation of p70 s6k by PDK1
Pullen, N., Dennis, P. B., Andjelkovic, M., Dufner, A., Kozma, S. C., Hemmings, B. A., & Thomas, G. (1998) · Science · doi:10.1126/science.279.5351.707 · Cited by 826
The glucose transporter family: structure, function and tissue-specific expression
Gould, G. W., & Holman, G. D. (1993) · Biochemical Journal · doi:10.1042/bj2950329 · Cited by 785
Phosphatidylinositol 3-Kinase Encoded by Yeast VPS 34 Gene Essential for Protein Sorting
Schu, P. V., Takegawa, K., Fry, M. J., Stack, J. H., Waterfield, M. D., & Emr, S. D. (1993) · Science · doi:10.1126/science.8385367 · Cited by 778
Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase
Otsu, M., Hiles, I., Gout, I. T., Fry, M., Ruiz‐Larrea, F., Panayotou, G., Thompson, A., Dhand, R., Hsuan, J. J., Totty, N. F., et al. (1991) · Cell · doi:10.1016/0092-8674(91)90411-q · Cited by 764
3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase
Alessi, D. R., Deák, M., Casamayor, A., Caudwell, F. B., MORRICE, N. A., Norman, D. G., Gaffney, P. R. J., Reese, C. B., MacDougall, C. N., Harbison, D., et al. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00336-8 · Cited by 754
Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3‐kinase inhibitors, wortmannin and LY294002.
Brunn, G. J., Williams, J. M., Sabers, C. J., Wiederrecht, G., Lawrence, J. C., & Abraham, R. T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00911.x · Cited by 715
PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase
Chung, J., Grammar, T. C., Lemon, K. P., Kazlauskas, A., & Blenis, J. (1994) · Nature · doi:10.1038/370071a0 · Cited by 712
Phosphoinositides as Regulators in Membrane Traffic
Camilli, P. V. D., Emr, S. D., McPherson, P. S., & Novick, P. (1996) · Science · doi:10.1126/science.271.5255.1533 · Cited by 706
Control of p70 S6 kinase by kinase activity of FRAP in vivo
Brown, E. J., Beal, P. A., Keith, C. T., Chen, J., Shin, T. B., & Schreiber, S. L. (1995) · Nature · doi:10.1038/377441a0 · Cited by 705
Phosphatidylinositol 3-kinase: Structure and expression of the 110 kd catalytic subunit
Hiles, I., Otsu, M., Volinia, S., Fry, M., Gout, I. T., Dhand, R., Panayotou, G., Ruiz‐Larrea, F., Thompson, A., Totty, N. F., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90166-a · Cited by 683
Cloning and Characterization of a G Protein-Activated Human Phosphoinositide-3 Kinase
Stoyanov, B., Volinia, S., Hanck, T., Rubio, I., Loubtchenkov, M., Malek, D., Stoyanova, S., Vanhaesebroeck, B., Dhand, R., Nürnberg, B., et al. (1995) · Science · doi:10.1126/science.7624799 · Cited by 674
A Grb2-associated docking protein in EGF- and insulin-receptor signalling
Holgado-Madruga, M., Emlet, D. R., Moscatello, D. K., Godwin, A. K., & Wong, A. J. (1996) · Nature · doi:10.1038/379560a0 · Cited by 672
Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
Kaplan, D. R., Whitman, M., Schaffhausen, B. S., Pallas, D. C., White, M. F., Cantley, L. C., & Roberts, T. M. (1987) · Cell · doi:10.1016/0092-8674(87)90168-1 · Cited by 646
Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
Valius, M., & Kazlauskas, A. (1993) · Cell · doi:10.1016/0092-8674(93)90232-f · Cited by 640
Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase‐1 and p70 S6 kinase
Alessi, D. R., Barry Caudwell, F., Andjelkovic, M., Hemmings, B. A., & Cohen, P. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01370-1 · Cited by 628
Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases
Skolnik, E. Y., Margolis, B. L., Mohammadi, M., Lowenstein, E. J., Fischer, R., Dreps, A., Ullrich, A., & Schlessinger, J. (1991) · Cell · doi:10.1016/0092-8674(91)90410-z · Cited by 627
3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
Alessi, D. R., Kozlowski, M. T., Weng, Q.-P., MORRICE, N. A., & Avruch, J. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70037-5 · Cited by 574
cDNA cloning of a Novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor
Escobedo, J. A., Navankasattusas, S., Kavanaugh, W. M., Milfay, D., Fried, V. A., & Williams, L. T. (1991) · Cell · doi:10.1016/0092-8674(91)90409-r · Cited by 573
Activation of phospholipase Cγ by PI 3‐kinase‐induced PH domain‐mediated membrane targeting
Falasca, M., Logan, S. K., Lehto, V. P., Baccante, G., Lemmon, M. A., & Schlessinger, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.414 · Cited by 567
Activation of phosphoinositide 3‐kinase by interaction with Ras and by point mutation.
Rodriguez‐Viciana, P., Warne, P. H., Vanhaesebroeck, B., Waterfield, M. D., & Downward, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00602.x · Cited by 566
Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.
Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M., Gout, I. T., Scaife, R. M., Margolis, R. L., Gigg, R., Smith, C. I., Driscoll, P. C., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01014.x · Cited by 562
The Gβγ Sensitivity of a PI3K Is Dependent upon a Tightly Associated Adaptor, p101
Stephens, L., Eguinoa, A., Erdjument‐Bromage, H., Lui, M. L., Cooke, F. T., Coadwell, J., Smrcka, A., Thelen, M., Cadwallader, K. A., Tempst, P., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80187-7 · Cited by 557
The GTPase dynamin binds to and is activated by a subset of SH3 domains
Gout, I. T., Dhand, R., Hiles, I. D., Fry, M., Panayotou, G., Das, P., Truong, O., Totty, N. F., Hsuan, J. J., Booker, G. W., et al. (1993) · Cell · doi:10.1016/s0092-8674(05)80081-9 · Cited by 557
Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.
Toker, A., Meyer, M., Reddy, K. K., Falck, J. R., Aneja, R., Aneja, S. G., Parra, A., Burns, D. J., Ballas, L. M., & Cantley, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31643-0 · Cited by 553
Ras-Dependent Induction of Cellular Responses by Constitutively Active Phosphatidylinositol-3 Kinase
Hu, Q., Klippel, A., Muslin, A. J., Fantl, W. J., & Williams, L. T. (1995) · Science · doi:10.1126/science.7701328 · Cited by 547
The Protein Kinase C Family for Neuronal Signaling
Tanaka, C., & Nishizuka, Y. (1994) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.17.030194.003003 · Cited by 543
PDGF stimulates an increase in GTP–Rac via activation of phosphoinositide 3-kinase
Hawkins, P. T., Eguinoa, A., Qiu, R., Stokoe, D., Cooke, F. T., Walters, R. J., Wennström, S., Claesson, L., Evans, T., Symons, M. H., et al. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00080-7 · Cited by 536
Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects.
Goodyear, L. J., Giorgino, F., Sherman, L., Carey, J., Smith, R. J., & Dohm, G. L. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117909 · Cited by 527
Wortmannin as a unique probe for an intracellular signalling protein, phosphoinositide 3-kinase
Ui, M., Okada, T., Hazeki, K., & Hazeki, O. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89056-8 · Cited by 520
Role of Phosphatidylinositol Kinase in PDGF Receptor Signal Transduction
Coughlin, S. R., Escobedo, J. A., & Williams, L. T. (1989) · Science · doi:10.1126/science.2466336 · Cited by 512
Activation of phosphatidylinositol 3-kinase by insulin.
Ruderman, N. B., Kapeller, R., White, M. F., & Cantley, L. C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1411 · Cited by 511
Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils
Stephens, L., Hughes, K. T., & Irvine, R. F. (1991) · Nature · doi:10.1038/351033a0 · Cited by 494
Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin
Lund, S., Holman, G. D., Schmitz, O., & Pedersen, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.5817 · Cited by 492
A Specific Product of Phosphatidylinositol 3-Kinase Directly Activates the Protein Kinase Akt through Its Pleckstrin Homology Domain
Klippel, A., Kavanaugh, W. M., Pot, D., & Williams, L. T. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.338 · Cited by 482
IRS-1 activates phosphatidylinositol 3'-kinase by associating with src homology 2 domains of p85.
Myers, M. G., Backer, J., Sun, X., Shoelson, S. E., Hu, P. J., Schlessinger, J., Yoakim, M., Schaffhausen, B. S., & White, M. F. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10350 · Cited by 480
The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
Cross, D. A. E., Alessi, D. R., Vandenheede, J. R., McDowell, H. E., Hundal, H. S., & Cohen, P. (1994) · Biochemical Journal · doi:10.1042/bj3030021 · Cited by 480
Pleiotropic Insulin Signals are Engaged by Multisite Phosphorylation of IRS-1
Sun, X., Crimmins, D. L., Myers, M. G., Miralpeix, M., & White, M. F. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7418 · Cited by 465
Phosphorylation and Activation of Heart 6-Phosphofructo-2-kinase by Protein Kinase B and Other Protein Kinases of the Insulin Signaling Cascades
Deprez, J., Vertommen, D., Alessi, D. R., Hue, L., & Rider, M. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17269 · Cited by 462
A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains
Rameh, L. E., Arvidsson, A., Carraway, K. L., Couvillon, A. D., Rathbun, G. A., Crompton, A. M., VanRenterghem, B., Czech, M., Ravichandran, K. S., Burakoff, S. J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22059 · Cited by 459
Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate
Stephens, L., Jackson, T., & Hawkins, P. T. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90072-w · Cited by 447
PI 3‐kinase is a dual specificity enzyme: autoregulation by an intrinsic protein‐serine kinase activity.
Dhand, R., Hiles, I., Panayotou, G., Roche, S., Fry, M., Gout, I. T., Totty, N. F., Truong, O., Vicendo, P., & Yonezawa, K. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06290.x · Cited by 446
p110δ, a novel phosphoinositide 3-kinase in leukocytes
Vanhaesebroeck, B., Welham, M. J., Kotani, K., Stein, R. C., Warne, P. H., Zvelebil, M., Higashi, K., Volinia, S., Downward, J., & Waterfield, M. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4330 · Cited by 445
Membrane Localization of Phosphatidylinositol 3-Kinase Is Sufficient To Activate Multiple Signal-Transducing Kinase Pathways
Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M.-A., & Williams, L. T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4117 · Cited by 440
Activation of the small GTP-binding proteins rho and rac by growth factor receptors
Nobes, C. D., Hawkins, P. T., Stephens, L., & Hall, A. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.1.225 · Cited by 438
Protein Kinase C-ζ as a Downstream Effector of Phosphatidylinositol 3-Kinase during Insulin Stimulation in Rat Adipocytes
Standaert, M. L., Galloway, L. C., Karnam, P., Bandyopadhyay, G. K., Moscat, J., & Farese, R. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30075 · Cited by 437
Activation of Phosphatidylinositol-3′ Kinase by Src-Family Kinase SH3 Binding to the p85 Subunit
Pleiman, C. M., Hertz, W., & Cambier, J. C. (1994) · Science · doi:10.1126/science.8128248 · Cited by 437
Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling
Wennström, S., Hawkins, P. T., Cooke, F. T., Hara, K., Yonezawa, K., Kasuga, M., Jackson, T., Claesson, L., & Stephens, L. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00087-7 · Cited by 436
Tumor Necrosis Factor α-induced Phosphorylation of Insulin Receptor Substrate-1 (IRS-1)
Kanety, H., Feinstein, R., Papa, M. Z., Hemi, R., & Karasik, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23780 · Cited by 435
1-Phosphatidylinositol 3-kinase activity is required for insulin-stimulated glucose transport but not for RAS activation in CHO cells.
Hara, K., Yonezawa, K., Sakaue, H., Ando, A., Kotani, K., Kitamura, T., Kitamura, Y., Ueda, H., Stephens, L., & Jackson, T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7415 · Cited by 433
p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity.
Lioubin, M. N., Algate, P. A., Tsai, S., Carlberg, K., Aebersold, A., & Rohrschneider, L. R. (1996) · Genes & Development · doi:10.1101/gad.10.9.1084 · Cited by 418
Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains
Klarlund, J. K., Guilherme, A., Holik, J. J., Virbasius, J. V., Chawla, A., & Czech, M. (1997) · Science · doi:10.1126/science.275.5308.1927 · Cited by 415
Transformation of Chicken Cells by the Gene Encoding the Catalytic Subunit of PI 3-Kinase
Chang, H. W., Aoki, M., Fruman, D. A., Auger, K. R., Bellacosa, A., Tsichlis, P. N., Cantley, L. C., Roberts, T. M., & Vogt, P. K. (1997) · Science · doi:10.1126/science.276.5320.1848 · Cited by 412
Cross-talk between the insulin and angiotensin signaling systems.
Velloso, L. A., Folli, F. B., Sun, X., White, M. F., Saad, M. J. A., & Kahn, C. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12490 · Cited by 402
Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
Welsh, G. I., & Proud, C. G. (1993) · Biochemical Journal · doi:10.1042/bj2940625 · Cited by 397
Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85.
Zheng, Y., Bagrodia, S., & Cerione, R. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32226-3 · Cited by 396
Physiological Role of Akt in Insulin-Stimulated Translocation of GLUT4 in Transfected Rat Adipose Cells
Cong, L.-N., Chen, H., Li, Y., Zhou, L., McGibbon, M. A., Taylor, S. I., & Quon, M. J. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.13.0027 · Cited by 386
Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit
Carpenter, C. L., Auger, K. R., Chanudhuri, M., Yoakim, M., Schaffhausen, B. S., Shoelson, S. E., & Cantley, L. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98375-4 · Cited by 384
A Novel 160-kDa Phosphotyrosine Protein in Insulin-treated Embryonic Kidney Cells Is a New Member of the Insulin Receptor Substrate Family
Lavan, B. E., Fantin, V. R., Chang, E. T., Lane, W. S., Keller, S. R., & Lienhard, G. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21403 · Cited by 381
Identification of Regulatory Phosphorylation Sites in Mitogen-activated Protein Kinase (MAPK)-activated Protein Kinase-1a/p90 That Are Inducible by MAPK
Dalby, K. N., MORRICE, N. A., Caudwell, F. B., Avruch, J., & Cohen, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1496 · Cited by 372
Insulin Receptor Substrate-1 Phosphorylation and Phosphatidylinositol 3-Kinase Activity in Skeletal Muscle From NIDDM Subjects After In Vivo Insulin Stimulation
Björnholm, M., Kawano, Y., Lehtihet, M., & Zierath, J. R. (1997) · Diabetes · doi:10.2337/diab.46.3.524 · Cited by 361
Inhibition of the translocation of GLUT1 and GLUT4 in 3T3-L1 cells by the phosphatidylinositol 3-kinase inhibitor, wortmannin
Clarke, J. F., Young, P. W., Yonezawa, K., Kasuga, M., & Holman, G. D. (1994) · Biochemical Journal · doi:10.1042/bj3000631 · Cited by 358
Potential Role of Protein Kinase B in Insulin-induced Glucose Transport, Glycogen Synthesis, and Protein Synthesis
Ueki, K., Yamamoto‐Honda, R., Kaburagi, Y., Yamauchi, T., Tobe, K., Burgering, B. M. T., Coffer, P. J., Komuro, I., Akanuma, Y., Yazaki, Y., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5315 · Cited by 357
Involvement of phosphoinositide 3‐kinase in insulin‐ or IGF‐1‐induced membrane ruffling.
Kotani, K., Yonezawa, K., Hara, K., Ueda, H., Kitamura, Y., Sakaue, H., Ando, A., Chavanieu, A., Calas, B., & Grigorescu, F. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06515.x · Cited by 355
The 60-kDa Phosphotyrosine Protein in Insulin-treated Adipocytes Is a New Member of the Insulin Receptor Substrate Family
Lavan, B. E., Lane, W. S., & Lienhard, G. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11439 · Cited by 353
An 81 kd protein complexed with middle T antigen and pp60c-src: A possible phosphatidylinositol kinase
Courtneidge, S. A., & Heber, A. (1987) · Cell · doi:10.1016/0092-8674(87)90169-3 · Cited by 345
Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
James, S. R., Downes, C. P., Gigg, R., Grove, S. J. A., Holmes, A. B., & Alessi, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3150709 · Cited by 341
A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids.
Nakanishi, S., Catt, K. J., & Balla, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5317 · Cited by 341
PI 3‐kinase: structural and functional analysis of intersubunit interactions.
Dhand, R., Hara, K., Hiles, I., Bax, B. D., Gout, I. T., Panayotou, G., Fry, M., Yonezawa, K., Kasuga, M., & Waterfield, M. D. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06289.x · Cited by 329
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
Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action
Eldar-Finkelman, H., & Krebs, E. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9660 · Cited by 319
The Effects of Wortmannin on Rat Skeletal Muscle
Yeh, J., Gulve, E. A., Rameh, L. E., & Birnbaum, M. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2107 · Cited by 313
New Insights Into the Role and Mechanism of Glycogen Synthase Activation by Insulin
Lawrence, J. C., & Roach, P. J. (1997) · Diabetes · doi:10.2337/diab.46.4.541 · Cited by 311
Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling.
Tanti, J., Grémeaux, T., OBBERGHEN, E. V., & MARCHAND‐BRUSTEL, Y. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37568-3 · Cited by 308
Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
Rameh, L. E., Chen, C., & Cantley, L. C. (1995) · Cell · doi:10.1016/0092-8674(95)90195-7 · Cited by 308
A human phosphatidylinositol 3‐kinase complex related to the yeast Vps34p‐Vps15p protein sorting system.
Volinia, S., Dhand, R., Vanhaesebroeck, B., MacDougall, L. K., Stein, R., Zvelebil, M. J., Domin, J., Panaretou, C., & Waterfield, M. D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07340.x · Cited by 307
Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin.
Schiavo, G., Gu, Q.-M., Prestwich, G., Söllner, T. H., & Rothman, J. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.23.13327 · Cited by 304
Construction and Characterization of a Conditionally Active Version of the Serine/Threonine Kinase Akt
Kohn, A. D., Barthel, A., Kovacina, K. S., Boge, A., Wallach, B. J., Summers, S. A., Birnbaum, M. J., Scott, P., Lawrence, J. C., & Roth, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11937 · Cited by 304
Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation and Function by Mitogen-activated Protein Kinase
De Fea, K., & Roth, R. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31400 · Cited by 298
Differential regulation of insulin receptor substrates-1 and -2 (IRS-1 and IRS-2) and phosphatidylinositol 3-kinase isoforms in liver and muscle of the obese diabetic (ob/ob) mouse.
Kerouz, N., Hörsch, D., Pons, S., & Kahn, C. R. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119872 · Cited by 296
Insulin receptor substrate (IRS) 1 is reduced and IRS-2 is the main docking protein for phosphatidylinositol 3-kinase in adipocytes from subjects with non-insulin-dependent diabetes mellitus
Rondinone, C. M., Wang, L.-M., Lönnroth, P., Wesslau, C., Pierce, J. H., & Smith, U. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4171 · Cited by 295
An inositol tetrakisphosphate-containing phospholipid in activated neutrophils
Traynor‐Kaplan, A., Harris, A. L., Thompson, B. L., Taylor, P., & Sklar, L. A. (1988) · Nature · doi:10.1038/334353a0 · Cited by 286
Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α
Walker, K. S., Deák, M., PATERSON, A., Hudson, K., Cohen, P., & Alessi, D. R. (1998) · Biochemical Journal · doi:10.1042/bj3310299 · Cited by 282
Insulin-Stimulated GLUT4 Translocation Is Relevant to the Phosphorylation of IRS-1 and the Activity of PI3 Kinase
Kanai, F., Ito, K., Todaka, M., Hayashi, H., Kamohara, S., Ishii, K., Okada, T., Hazeki, O., Ui, M., & Ebina, Y. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2111 · Cited by 281
Insulin stimulation of glycogen synthesis and glycogen synthase activity is blocked by wortmannin and rapamycin in 3T3-L1 adipocytes: evidence for the involvement of phosphoinositide 3-kinase and p70 ribosomal protein-S6 kinase
Shepherd, P. R., Navé, B. T., & Siddle, K. (1995) · Biochemical Journal · doi:10.1042/bj3050025 · Cited by 277
Self-citation
Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways
Rei, K., Nobes, C. D., Thomas, G., Hall, A., & Cantrell, D. A. (1996) · Current Biology · doi:10.1016/s0960-9822(96)00749-x · Cited by 276
The IRS‐signalling system during insulin and cytokine action
Yenush, L., & White, M. F. (1997) · BioEssays · doi:10.1002/bies.950190608 · Cited by 273
EGF or PDGF receptors activate atypical PKClambda through phosphatidylinositol 3‐kinase.
Akimoto, K., Takahashi, R., Moriya, S., Nishioka, N., Takayanagi, J., Kimura, K. D., Fukui, Y., Osada, S.-I., Mizuno, K., Hirai, S., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00414.x · Cited by 269
Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3‐kinase
Jiménez, C., Jones, D. R., Rodriguez‐Viciana, P., González-Garcı́a, A., Leonardo, E., Wennström, S., von Kobbe, C., Toran, J. L., R‐Borlado, L., Calvo, V., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.3.743 · Cited by 269
Regulatory intramolecular association in a tyrosine kinase of the Tec family
Andreotti, A. H., Bunnell, S. C., Feng, S., Berg, L. J., & Schreiber, S. L. (1997) · Nature · doi:10.1038/385093a0 · Cited by 268
The phosphatidylinositol 3-kinase alpha is required for DNA synthesis induced by some, but not all, growth factors.
Roche, S., Koegl, M., & Courtneidge, S. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9185 · Cited by 267
Regulation of translation elongation factor‐2 by insulin via a rapamycin‐sensitive signalling pathway.
Redpath, N. T., Foulstone, E. J., & Proud, C. G. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00582.x · Cited by 265
Cloning of a Novel, Ubiquitously Expressed Human Phosphatidylinositol 3-Kinase and Identification of Its Binding Site on p85
Hu, P. J., Mondino, A., Skolnik, E. Y., & Schlessinger, J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7677 · Cited by 261
Potential Role of Protein Kinase B in Glucose Transporter 4 Translocation in Adipocytes
Tanti, J., Grillo, S., Grémeaux, T., Coffer, P. J., OBBERGHEN, E. V., & MARCHAND‐BRUSTEL, Y. L. (1997) · Endocrinology · doi:10.1210/endo.138.5.5136 · Cited by 260
Phosphatidylinositol kinase or an associated protein is a substrate for the insulin receptor tyrosine kinase.
Endemann, G., Yonezawa, K., & Roth, R. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40243-3 · Cited by 257
Molecular mechanisms for the control of translation by insulin
Proud, C. G., & DENTON, M. R. (1997) · Biochemical Journal · doi:10.1042/bj3280329 · Cited by 257
Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries.
Rickles, R. J., Botfield, M. C., Weng, Z., Taylor, J. A., Green, O. M., Brugge, J. S., & Zoller, M. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06897.x · Cited by 256
Phosphorylation of Insulin Receptor Substrate-1 on Multiple Serine Residues, 612, 632, 662, and 731, Modulates Insulin Action
Mothe‐Satney, I., & OBBERGHEN, E. V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11222 · Cited by 254
Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
Jan Domin, Y., Pagès, F., Volinia, S., Rittenhouse-Simmons, S., Zvelebil, M., Stein, R. C., & Waterfield, M. D. (1997) · Biochemical Journal · doi:10.1042/bj3260139 · Cited by 251
Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
Kanamarlapudi, V., Oatey, P. B., Tavaré, J. M., & Cullen, P. J. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70181-2 · Cited by 251
Platelet-derived growth factor stimulates synthesis of Ptdlns(3,4,5)P3 by activating a Ptdlns(4,5)P2 3-OH kinase
Hawkins, P. T., Jackson, T., & Stephens, L. (1992) · Nature · doi:10.1038/358157a0 · Cited by 248
Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase.
Kazlauskas, A., & Cooper, J. A. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07527.x · Cited by 247
Wortmannin and Its Structural Analogue Demethoxyviridin Inhibit Stimulated Phospholipase A2 Activity in Swiss 3T3 Cells
Cross, M. J., Stewart, A., Hodgkin, M. N., Kerr, D. J., & Wakelam, M. J. O. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25352 · Cited by 246
Insulin Increases the Association of Akt-2 with Glut4-containing Vesicles
Calera, M. R., Martı́nez, C., Liu, H., Jack, A. K. E., Birnbaum, M. J., & Pilch, P. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7201 · Cited by 244
Growth Hormone, Interferon-γ, and Leukemia Inhibitory Factor Promoted Tyrosyl Phosphorylation of Insulin Receptor Substrate-1
Argetsinger, L. S., Hsu, G. W., Myers, M. G., Billestrup, N., White, M. F., & Carter‐Su, C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14685 · Cited by 244
Protein Kinase C Modulation of Insulin Receptor Substrate-1 Tyrosine Phosphorylation Requires Serine 612
Fea, K. D., & Roth, R. A. (1997) · Biochemistry · doi:10.1021/bi971157f · Cited by 242
Identification of a Second SH2-Domain-Containing Protein Closely Related to the Phosphatidylinositol Polyphosphate 5-Phosphatase SHIP
Pesesse, X., Deleu, S., Smedt, F. D., Drayer, L., & Erneux, C. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7538 · Cited by 240
The Structure and Function of P55 PIK Reveal a New Regulatory Subunit for Phosphatidylinositol 3-Kinase
Pons, S., Asano, T., Glasheen, E. M., Miralpeix, M., Zhang, Y., Fisher, T. L., Myers, M. G., Sun, X., & White, M. F. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4453 · Cited by 240
The α‐isoform of glycogen synthase kinase‐3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase‐activated protein kinase‐1 in vitro
Sutherland, C. D., & Cohen, P. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80112-6 · Cited by 237
4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase.
von Manteuffel, S. R., Gingras, A., Ming, X., Sonenberg, N., & Thomas, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4076 · Cited by 235
The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-1. Stimulation by insulin and inhibition by Wortmannin.
Lam, K., Carpenter, C. L., Ruderman, N. B., Friel, J., & Kelly, K. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32042-2 · Cited by 232
Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase.
Guinebault, C., Payrastre, B., Racaud‐Sultan, C., Mazarguil, H., Breton, M., Mauco, G., Plantavid, M. M., & Chap, H. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.3.831 · Cited by 227
Regulation of Phosphatidylinositol 3′-Kinase by Tyrosyl Phosphoproteins
Rordorf-Nikolic, T., Horn, D. J. V., Chen, D., White, M. F., & Backer, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.8.3662 · Cited by 226
Rapamycin inhibits clonal expansion and adipogenic differentiation of 3T3-L1 cells.
Yeh, W., Bierer, B. E., & McKnight, S. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.11086 · Cited by 226
PTB Domains of IRS-1 and Shc Have Distinct but Overlapping Binding Specificities
Wolf, G., Trüb, T., Ottinger, E. A., Groninga, L., Lynch, A., White, M. F., Miyazaki, M., Lee, J., & Shoelson, S. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27407 · Cited by 223
Tandem SH2 Domains Confer High Specificity in Tyrosine Kinase Signaling
Ottinger, E. A., Botfield, M. C., & Shoelson, S. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.729 · Cited by 223
R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways
Marte, B. M., Rodriguez-Viciana, P., Wennström, S., Warne, P. H., & Downward, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00028-5 · Cited by 223
Insulin activates protein kinase B, inhibits glycogen synthase kinase‐3 and activates glycogen synthase by rapamycin‐insensitive pathways in skeletal muscle and adipose tissue
Cross, D. A. E., Watt, P., Shaw, M., KAAY, J. V. D., Downes, C. P., Holder, J. C., & Cohen, P. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00240-8 · Cited by 221
Regulation of phosphatidylinositol 3-kinase activity in liver and muscle of animal models of insulin-resistant and insulin-deficient diabetes mellitus.
Folli, F. B., Saad, M. J. A., Backer, J., & Kahn, C. R. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116768 · Cited by 220
Evidence for Involvement of Protein Kinase C (PKC)-ζ and Noninvolvement of Diacylglycerol-Sensitive PKCs in Insulin-Stimulated Glucose Transport in L6 Myotubes*
Bandyopadhyay, G. K., Standaert, M. L., Galloway, L. C., Moscat, J., & Farese, R. V. (1997) · Endocrinology · doi:10.1210/endo.138.11.5473 · Cited by 218
From receptor to transporter: insulin signalling to glucose transport
Holman, G. D., & Kasuga, M. (1997) · Diabetologia · doi:10.1007/s001250050780 · Cited by 215
B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
Murata, K., Wu, J., & Brautigan, D. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10624 · Cited by 213
Insulin-stimulated phosphatidylinositol 3-kinase. Association with a 185-kDa tyrosine-phosphorylated protein (IRS-1) and localization in a low density membrane vesicle.
Kelly, K. L., & Ruderman, N. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53622-x · Cited by 211
Differential Signaling by Insulin Receptor Substrate 1 (IRS-1) and IRS-2 in IRS-1-Deficient Cells
Brüning, J. C., Winnay, J. N., Cheatham, B., & Kahn, C. R. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1513 · Cited by 206
A Tightly Associated Serine/Threonine Protein Kinase Regulates Phosphoinositide 3-Kinase Activity
Carpenter, C. L., Auger, K. R., Duckworth, B. C., Hou, W., Schaffhausen, B. S., & Cantley, L. C. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.3.1657-1665.1993 · Cited by 205
Phosphatidylinositol 3-kinase signals activation of p70 S6 kinase in situ through site-specific p70 phosphorylation.
Weng, Q. P., Andrabi, K. I., Klippel, A., Kozlowski, M. T., Williams, L. T., & Avruch, J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5744 · Cited by 204
Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase
Welsh, G. I., Foulstone, E. J., Young, S. W., Tavaré, J. M., & Proud, C. G. (1994) · Biochemical Journal · doi:10.1042/bj3030015 · Cited by 201
p70 S6 kinase: an enigma with variations
Proud, C. G. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10016-5 · Cited by 201
Overexpression of Catalytic Subunit p110α of Phosphatidylinositol 3-Kinase Increases Glucose Transport Activity with Translocation of Glucose Transporters in 3T3-L1 Adipocytes
Katagiri, H., Asano, T., Ishihara, H., Inukai, K., Shibasaki, Y., Kikuchi, M., Yazaki, Y., & Oka, Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.16987 · Cited by 194
Rac GTPase interacts specifically with phosphatidylinositol 3-kinase
Bokoch, G., Vlahos, C. J., Wang, Y., Knaus, U. G., & Traynor‐Kaplan, A. (1996) · Biochemical Journal · doi:10.1042/bj3150775 · Cited by 188
Altered Expression Levels and Impaired Steps in the Pathway to Phosphatidylinositol 3-Kinase Activation via Insulin Receptor Substrates 1 and 2 in Zucker Fatty Rats
Anai, M., Funaki, M., Ogihara, T., Terasaki, J., Inukai, K., Katagiri, H., Fukushima, Y., Yazaki, Y., Kikuchi, M., Oka, Y., et al. (1998) · Diabetes · doi:10.2337/diab.47.1.13 · Cited by 180
The v-Src SH3 Domain Binds Phosphatidylinositol 3'-Kinase
Liu, X. J., Marengère, L. E. M., Koch, C. A., & Pawson, T. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5225 · Cited by 178
Association of p21ras with phosphatidylinositol 3-kinase.
Sjölander, A., Yamamoto, K., Huber, B. E., & Lapetina, E. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.18.7908 · Cited by 177
The Pleckstrin Homology Domain Is the Principle Link between the Insulin Receptor and IRS-1
Yenush, L., Makati, K. J., Smith-Hall, J., Ishibashi, O., Myers, M. G., & White, M. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.24300 · Cited by 177
Differential Effects of Constitutively Active Phosphatidylinositol 3-Kinase on Glucose Transport, Glycogen Synthase Activity, and DNA Synthesis in 3T3-L1 Adipocytes
Frevert, E. U., & Kahn, B. B. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.190 · Cited by 170
Expression of a constitutively activated form of protein kinase B (c- Akt) in 3T3-L1 preadipose cells causes spontaneous differentiation
Magun, R., Burgering, B. M. T., Coffer, P. J., Pardasani, D., Lin, Y.-T., Chabot, J., & Sorisky, A. (1996) · Endocrinology · doi:10.1210/endo.137.8.8754791 · Cited by 167
Intracellular Localization of Phosphatidylinositide 3-kinase and Insulin Receptor Substrate-1 in Adipocytes: Potential Involvement of a Membrane Skeleton
Clark, S. F., Martin, S., Carozzi, A., Hill, M. M. C., & James, D. E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.5.1211 · Cited by 167
Platelet-derived growth factor activates protein kinase C epsilon through redundant and independent signaling pathways involving phospholipase C gamma or phosphatidylinositol 3-kinase.
Moriya, S., Kazlauskas, A., Akimoto, K., Hirai, S.-I., Mizuno, K., Takenawa, T., Fukui, Y., Watanabe, Y., Ozaki, S., & Ohno, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.151 · Cited by 166
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase.
Shoelson, S. E., Chatterjee, S., Chaudhuri, M. K., & White, M. F. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2027 · Cited by 166
p85α Gene Generates Three Isoforms of Regulatory Subunit for Phosphatidylinositol 3-Kinase (PI 3-Kinase), p50α, p55α, and p85α, with Different PI 3-Kinase Activity Elevating Responses to Insulin
Inukai, K., Funaki, M., Ogihara, T., Katagiri, H., Kanda, A., Anai, M., Fukushima, Y., Hosaka, T., Suzuki, M., Shin, B., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7873 · Cited by 166
The insulin and insulin-like growth factor-I receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro.
Giorgetti‐Peraldi, S., Ballotti, R., Kowalski‐Chauvel, A., Tartare‐Deckert, S., & OBBERGHEN, E. V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53183-5 · Cited by 165
A Functional Phosphatidylinositol 3,4,5-Trisphosphate/Phosphoinositide Binding Domain in the Clathrin Adaptor AP-2 α Subunit. IMPLICATIONS FOR THE ENDOCYTIC PATHWAY
Gaidarov, I., Chen, Q., Falck, J. R., Reddy, K. K., & Keen, J. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20922 · Cited by 165
Receptor stimulated accumulation of phosphatidylinositol (3,4,5)‐trisphosphate by G‐protein mediated pathways in human myeloid derived cells.
Stephens, L., Eguinoa, A., Corey, S., Jackson, T., & Hawkins, P. T. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05880.x · Cited by 162
Activation of pp70/85 S6 Kinases in Interleukin-2-Responsive Lymphoid Cells Is Mediated by Phosphatidylinositol 3-Kinase and Inhibited by Cyclic AMP
Monfar, M., Lemon, K. P., Grammer, T. C., Cheatham, L. A., Chung, J., Vlahos, C. J., & Blenis, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.326 · Cited by 161
Multiple roles of phosphatidylinositol 3-kinase in regulation of glucose transport, amino acid transport, and glucose transporters in L6 skeletal muscle cells
Tsakiridis, T. K., McDowell, H. E., Walker, T. R., Downes, C. P., Hundal, H. S., Vranić, M., & Klip, A. (1995) · Endocrinology · doi:10.1210/endo.136.10.7664650 · Cited by 158
Signaling Pathways through Which Insulin Regulates CCAAT/Enhancer Binding Protein α (C/EBPα) Phosphorylation and Gene Expression in 3T3-L1 Adipocytes
Hemati, N., Ross, S. E., Erickson, R. L., Groblewski, G. E., & MacDougald, O. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25913 · Cited by 158
Overexpression of a Constitutively Active Form of Phosphatidylinositol 3-Kinase Is Sufficient to Promote Glut 4 Translocation in Adipocytes
Tanti, J., Grémeaux, T., Grillo, S., Calleja, V., Klippel, A., Williams, L. T., OBBERGHEN, E. V., & MARCHAND‐BRUSTEL, Y. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25227 · Cited by 156
Involvement of p85 in p53-dependent apoptotic response to oxidative stress
Yin, Y., Terauchi, Y., Solomon, G. G., Aizawa, S., Rangarajan, P. N., Yazaki, Y., Kadowaki, T., & Barrett, J. C. (1998) · Nature · doi:10.1038/35648 · Cited by 155
Mouse p170 Is a Novel Phosphatidylinositol 3-Kinase Containing a C2 Domain
Virbasius, J. V., Guilherme, A., & Czech, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13304 · Cited by 154
Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3'-kinase. Formation of binary and ternary signaling complexes in intact cells.
Backer, J., Myers, M. G., Sun, X., Chin, D. J., Shoelson, S. E., Miralpeix, M., & White, M. F. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53083-0 · Cited by 153
Regulation of Both Glycogen Synthase and PHAS-I by Insulin in Rat Skeletal Muscle Involves Mitogen-activated Protein Kinase-independent and Rapamycin-sensitive Pathways
Azpiazu, I., Saltiel, A. R., DePaoli-Roach, A. A., & Lawrence, J. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.5033 · Cited by 152
Interactions Between SH2 Domains and Tyrosine-Phosphorylated Platelet-Derived Growth Factor β-receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor-Based Approach
Panayotou, G., Gish, G., End, P., Truong, O., Gout, I. T., Dhand, R., Fry, M., Hiles, I., Pawson, T. J., & Waterfield, M. D. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3567 · Cited by 150
Activation of Mitogen-activated Protein Kinase and Phosphatidylinositol 3′-Kinase Is Not Sufficient for the Hormonal Stimulation of Glucose Uptake, Lipogenesis, or Glycogen Synthesis in 3T3-L1 Adipocytes
Wiese, R. J., Mastick, C. C., Lazar, D. F., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3442 · Cited by 150
The inability of phosphatidylinositol 3-kinase activation to stimulate GLUT4 translocation indicates additional signaling pathways are required for insulin-stimulated glucose uptake.
Isakoff, S. J., Taha, C., Rose, E., Marcusohn, J., Klip, A., & Skolnik, E. Y. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10247 · Cited by 149
Membrane-permeant Esters of Phosphatidylinositol 3,4,5-Trisphosphate
Jiang, T., Sweeney, G., Rudolf, M. T., Klip, A., Traynor‐Kaplan, A., & Tsien, R. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.11017 · Cited by 148

Research works printed but not linked: 21

Nakanishi, S., Catt, K. J. and Balla, T. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 5317-5321
Hara, K., Yonezawa, K., Sakaue, H., Ando, A., Kotani, K., Kitamura, T., Kitamura, Y., Ueda, H., Stephens, L., Jackson, T. R. et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 7415-7419
Vanhaesebroeck, B., Welham, M. J., Kotani, K., Stein, R., Warne, P. H., Zvelebil, M. J., Higashi, K., Volinia, S., Downward, J. and Waterfield, M. D. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 4330-4335 48
Shoelson, S. E., Chatterjee, S., Chaudhuri, M. and White, M. F. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2027-2031 100
Myers, M. G., Backer, J. M., Sun, X. J., Shoelson, S., Hu, P., Schlessinger, J., Yoakim, M., Schaffhausen, B. and White, M. F. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 10350-10354 115
Eldar-Finkelman, H. and Krebs, E. G. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 9660-9664 130
Ruderman, N. B., Kapeller, R., White, M. F. and Cantley, L. C. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 1411-1415 143
Roche, S., Koegl, M. and Courtneidge, S. A. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 9185-9189 156
Oka, Y., Mottola, C., Oppenheimer, C. L. and Czech, M. P. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 4028-4032 161
Sjolander, A., Yamamoto, K., Huber, B. E. and Lapetina, E. G. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 7908-7912 162
Schiavo, G., Gu, Q., Prestwich, G. D., Sollner, T. H. and Rothman, J. E. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 13327-13332 182
Weng, Q. P., Andrabi, K., Klippel, A., Kozlowski, M. T., Williams, L. T. and Avruch, J. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 5744-5748 220
Burnett, P. E., Barrow, R. K., Cohen, N. A., Snyder, S. H. and Sabatini, D. M. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 1432-1437 229
Moriya, S., Kazlauskas, A., Akimoto, K., Hirai, S., Mizuno, K., Takenawa, T., Fukui, Y., Watanabe, Y., Ozaki, S. and Ohno, S. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 151-155 231
Yeh, W., Bierer, B. E. and McKnight, S. L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 11086-11090 251
Lund, S., Holman, G. D., Schmitz, O. and Pedersen, O. (1995) Proc. Natl. Acad. Sci.
Maruta, K., Wu, J. and Brautigan, D. L. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 10624-10629 297
Von-Manteuffel, S. R., Gingras, A. C., Ming, X. F., Sonenberg, N. and Thomas, G. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 4076-4080 313
Isakoff, S. J., Taha, C., Rose, E., Marcusohn, J., Klip, A. and Skolnik, E. Y. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 10247-10251 324
Velloso, L. A., Folli, F., Sun, X. J., White, M. F., Saad, M. J. and Kahn, C. R. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 12490-12495 325
Rondinone, C. M., Wang, L., Lonnroth, P., Wesslau, C., Pierce, J. H. and Smith, U. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 4171-4175 334

Sorted by citations

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
The PI3K‒PDK1 connection: more than just a road to PKB
Vanhaesebroeck, B., & Alessi, D. R. (2000) · Biochemical Journal · doi:10.1042/bj3460561 · Cited by 1,649
Synthesis and Function of 3-Phosphorylated Inositol Lipids
Vanhaesebroeck, B., Leevers, S. J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P. C., Woscholski, R., Parker, P. J., & Waterfield, M. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.535 · Cited by 1,535
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
Self-citation
Cellular Function of Phosphoinositide 3-Kinases: Implications for Development, Immunity, Homeostasis, and Cancer
Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J. F., & Waterfield, M. D. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.615 · Cited by 1,230

See all 953

Authors: SHEPHERD, P. R., WITHERS, D. J., & SIDDLE, K.
Affiliations: University College London (GB)
Joslin Diabetes Center (US)
University of Cambridge (GB)
ORCID: SHEPHERD, Peter R.
WITHERS, Dominic J.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1998-08-01
Volume: 333
Issue: 3
Pages: 471-490
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3330471
PMC: PMC1219607
OpenAlex: W1841050729
Cited by: 953
References: 338
Citations by year: 2026: 5 · 2025: 4 · 2024: 7 · 2023: 13 · 2022: 15 · 2021: 7 · 2020: 22 · 2019: 19 · 2018: 13 · 2017: 16 · 2016: 18 · 2015: 29 · 2014: 21 · 2013: 15 · 2012: 31
FWCI: 6.22
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
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
Keywords: phosphatidylinositol 3-kinase, insulin signaling, insulin receptor, phosphoinositide 3-phosphate, pleckstrin homology domain, Akt, allosteric regulation, lipid second messengers, glucose metabolism, lipid metabolism
MeSH terms: Animals, Humans, Insulin, Signal Transduction, Phosphatidylinositol 3-Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks