AKT/PKB and Other D3 Phosphoinositide-Regulated Kinases: Kinase Activation by Phosphoinositide-Dependent Phosphorylation

Chan, Tung O.; Rittenhouse, Susan E.; Tsichlis, Philip N.

doi:10.1146/annurev.biochem.68.1.965

Cited by 737

The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.

AKT/PKB and Other D3 Phosphoinositide-Regulated Kinases: Kinase Activation by Phosphoinositide-Dependent Phosphorylation

Chan, Tung O., Rittenhouse, Susan E., Tsichlis, Philip N.·1999·Annual Review of Biochemistry

DOI 10.1146/annurev.biochem.68.1.965

Open this paper in CoChat — free account

Abstract

▪ Abstract The protein kinase Akt/PKB is activated via a multistep process by a variety of signals. In the early steps of this process, PI-3 kinase-generated D3-phosphorylated phosphoinositides bind the Akt PH domain and induce the translocation of the kinase to the plasma membrane where it co-localizes with phosphoinositide-dependent kinase-1. By binding to the PH domains of both Akt and phosphoinositide-dependent kinase-1, D3-phosphorylated phosphoinositides appear to also induce conformational changes that permit phosphoinositide-dependent kinase-1 to phosphorylate the activation loop of Akt. The paradigm of Akt activation via phosphoinositide-dependent phosphorylation provided a framework for research into the mechanism of activation of other members of the AGC kinase group (p70 S6K, PKC, and PKA) and members of the Tec tyrosine kinase family (TecI, TecII, Btk/Atk, Itk/Tsk/Emt, Txk/Rlk, and Bm/Etk). The result was the discovery that these kinases and Akt are activated by overlapping pathways. In this review, we present our current understanding of the regulation and function of the Akt kinase and we discuss the common and unique features of the activation processes of Akt and the AGC and Tec kinase families. In addition, we present an overview of the biosynthesis of phosphoinositides that contribute to the regulation of these kinases.

Integrity signals

Registry

Crossref · 10.1146/annurev.biochem.68.1.965

Cites

12 of 12 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

AKT plays an important role in the regulation of cell survival signals in response to deprivation of growth factors, cytokines, and oncogenic Ras.
“AKT has been shown to play an important role in the regulation of cell survival signals in response to deprivation of growth factors, cytokines, and oncogenic Ras (76”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [76]

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
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104
Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130
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
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
FYVE fingers bind PtdIns(3)P
Gaullier, J.-M., Simonsen, A., D'Arrigo, A., Bremnes, B., Stenmark, H., & Aasland, R. (1998) · Nature · doi:10.1038/28767 · Cited by 553
TOR signalling and control of cell growth
Thomas, G., & Hall, M. N. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80078-6 · Cited by 462
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
Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ
Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30491 · Cited by 378
Constitutive activation of protein kinase B alpha by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells.
Hajduch, E., Alessi, D. R., Hemmings, B. A., & Hundal, H. S. (1998) · Diabetes · doi:10.2337/diabetes.47.7.1006 · Cited by 335
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
Phospholipid-binding protein domains
Bottomley, M. J., Salim, K., & Panayotou, G. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00141-6 · Cited by 118

Flagged first, then by citations

Research works printed but not linked: 324

10.1210/er.17.6.698 · DOI
10.1146/annurev.ph.56.030194.001321 · DOI
10.1016/0092-8674(95)90408-5 · DOI
10.1016/0092-8674(95)90409-3 · DOI
10.1074/jbc.270.22.12949 · DOI · Paper page
10.1016/S0955-0674(97)80059-2 · DOI
10.1016/0955-0674(93)90116-8 · DOI
Dennis EA, 1995, Adv. Prostaglandin Thromboxane Leukot. Res., 23, 75
10.1074/jbc.274.7.3919 · DOI
10.1016/S0005-2760(98)00146-5 · DOI
10.1016/S0005-2760(98)00139-8 · DOI
10.1146/annurev.biochem.67.1.481 · DOI
10.1038/376599a0 · DOI
10.1016/0092-8674(95)90534-0 · DOI
10.1002/j.1460-2075.1995.tb00103.x · DOI
10.1038/42648 · DOI
10.1096/fasebj.9.8.7768349 · DOI
10.1006/smim.1995.0028 · DOI
10.1016/S0005-2760(98)00134-9 · DOI
10.1016/S0005-2760(98)00140-4 · DOI
10.1074/jbc.273.1.13 · DOI
10.1016/0092-8674(92)90166-A · DOI
10.1128/MCB.13.12.7677 · DOI
10.1073/pnas.94.9.4330 · DOI
10.1042/bj3240489 · DOI
Kucera GL, 1990, J. Biol. Chem., 265, 5345, 10.1016/S0021-9258(19)39361-5 · DOI
10.1128/MCB.16.4.1722 · DOI
Vlahos CJ, 1995, J. Immunol., 154, 2413, 10.4049/jimmunol.154.5.2413 · DOI
10.1016/0092-8674(91)90411-Q · DOI
10.1002/j.1460-2075.1994.tb06289.x · DOI
10.1128/MCB.15.8.4453 · DOI
10.1074/jbc.271.10.5317 · DOI
10.1128/MCB.16.5.2195 · DOI
10.1074/jbc.272.12.7873 · DOI
10.1016/S0092-8674(00)80187-7 · DOI
10.1126/science.283.5400.393 · DOI · Paper page
10.1126/science.283.5400.390 · DOI
10.1006/geno.1996.0527 · DOI
Kaibuchi K, 1989, J. Biol. Chem., 264, 13489, 10.1016/S0021-9258(18)80023-0 · DOI
10.1074/jbc.271.23.13892 · DOI
10.1074/jbc.271.23.13304 · DOI
10.1042/bj3260139 · DOI
10.1006/bbrc.1997.6495 · DOI
10.1074/jbc.273.49.33082 · DOI
10.1016/S0960-9822(95)00278-8 · DOI
10.1074/jbc.273.23.14081 · DOI
10.1002/j.1460-2075.1995.tb07340.x · DOI · Paper page
Stack JH, 1994, J. Biol. Chem., 269, 31552, 10.1016/S0021-9258(18)31729-0 · DOI
10.1074/jbc.272.4.2477 · DOI
10.1038/ng1095-115 · DOI
10.1038/371297a0 · DOI
10.1016/S0955-0674(98)80067-7 · DOI
10.1128/MCB.13.3.1657 · DOI
10.1002/j.1460-2075.1994.tb06290.x · DOI
Lam K, 1994, J. Biol. Chem., 269, 20648, 10.1016/S0021-9258(17)32042-2 · DOI
10.1126/science.282.5387.293 · DOI
10.1016/S0968-0004(97)01120-1 · DOI
10.1016/S0005-2760(98)00132-5 · DOI
10.1016/0014-5793(94)00509-5 · DOI
Laxminarayan KM, 1994, J. Biol. Chem., 269, 17305, 10.1016/S0021-9258(17)32555-3 · DOI
10.1074/jbc.272.9.5983 · DOI
10.1038/376527a0 · DOI
10.1002/j.1460-2075.1996.tb00866.x · DOI
10.1038/358239a0 · DOI
10.1002/j.1460-2075.1995.tb00128.x · DOI
10.1074/jbc.272.9.5983 · DOI
10.1016/S0960-9822(02)00511-0 · DOI · Paper page
10.1016/S0014-5793(98)01255-1 · DOI
10.1006/geno.1995.1247 · DOI
10.1073/pnas.93.4.1689 · DOI · Paper page
10.1006/bbrc.1996.1161 · DOI
10.1074/jbc.271.51.32689 · DOI
10.1016/S0092-8674(00)80337-2 · DOI
10.1093/emboj/17.7.1961 · DOI
10.1016/S1074-7613(00)80555-5 · DOI
10.1038/387101a0 · DOI
10.1038/379353a0 · DOI
10.1074/jbc.272.49.30817 · DOI
10.1074/jbc.273.4.2306 · DOI
Srinivasan S, 1997, Eur. J. Cell. Biol., 74, 350
10.1074/jbc.270.44.26619 · DOI
10.1074/jbc.272.13.8710 · DOI
10.1126/science.275.5308.1943 · DOI · Paper page
10.1038/ng0497-356 · DOI
Tashiro H, 1997, Cancer Res., 57, 3935
Cairns P, 1997, Cancer Res., 57, 4997
Guldberg P, 1997, Cancer Res., 57, 3660
Dahia PL, 1997, Cancer Res., 57, 4710
10.1038/ng0597-64 · DOI
10.1038/ng0897-333 · DOI
10.1002/(SICI)1096-8628(19970905)71:4<489::AID-AJMG24>3.3.CO;2-I · DOI
10.1038/1235 · DOI
10.1016/S0960-9822(07)00488-5 · DOI
10.1016/S0968-0004(96)10059-1 · DOI
10.1126/science.280.5369.1614 · DOI · Paper page
10.1016/S0092-8674(00)81780-8 · DOI · Paper page
10.1016/S0960-9822(07)00493-9 · DOI
Davies MA, 1998, Cancer Res., 58, 5285
10.1073/pnas.95.26.15587 · DOI · Paper page
10.1073/pnas.95.23.13513 · DOI
10.1016/0092-8674(95)90525-1 · DOI
10.1016/S0962-8924(98)01281-1 · DOI
10.1038/347561a0 · DOI
10.1073/pnas.92.1.112 · DOI
10.1016/0092-8674(91)90508-V · DOI
10.1038/374173a0 · DOI · Paper page
10.1016/S0896-6273(00)80312-8 · DOI
10.1016/S0092-8674(00)81022-3 · DOI
10.1146/annurev.biophys.27.1.503 · DOI
10.1038/371168a0 · DOI
10.1074/jbc.272.35.22059 · DOI
10.1002/j.1460-2075.1996.tb01014.x · DOI
10.1042/bj3150709 · DOI
10.1126/science.279.5351.710 · DOI
10.1111/j.1432-1033.1997.00512.x · DOI
10.1074/jbc.271.31.18859 · DOI
10.1126/science.275.5308.1927 · DOI
10.1126/science.279.5350.558 · DOI
10.1016/0959-440X(93)90145-B · DOI
10.1016/0092-8674(95)90195-7 · DOI
10.1074/jbc.273.37.23750 · DOI
10.1074/jbc.273.8.4465 · DOI · Paper page
10.1038/378584a0 · DOI
10.1016/S0092-8674(00)81236-2 · DOI
10.1002/pro.5560051201 · DOI
10.1073/pnas.93.23.13327 · DOI
10.1128/MCB.19.1.623 · DOI
10.1093/emboj/16.9.2240 · DOI
10.1074/jbc.272.1.466 · DOI
10.1038/35882 · DOI
10.1126/science.273.5277.956 · DOI
10.1073/pnas.74.7.3065 · DOI
10.1073/pnas.84.14.5034 · DOI
10.1126/science.1833819 · DOI
10.1111/j.1432-1033.1991.tb16305.x · DOI
10.1073/pnas.88.10.4171 · DOI
10.1091/mbc.2.12.1001 · DOI
10.1073/pnas.89.19.9267 · DOI
10.1006/bbrc.1995.2654 · DOI
10.1128/MCB.17.1.338 · DOI
10.1126/science.277.5325.567 · DOI
10.1073/pnas.94.25.13820 · DOI
10.1073/pnas.94.21.11227 · DOI
10.1073/pnas.95.7.3644 · DOI
10.1016/S0960-9822(06)00122-9 · DOI
10.1038/sj.onc.1201947 · DOI
10.1016/S0960-9822(06)00336-8 · DOI
10.1016/S0960-9822(98)70037-5 · DOI
10.1042/bj3320281 · DOI
10.1073/pnas.95.17.9849 · DOI
10.1074/jbc.271.48.30835 · DOI
10.1128/MCB.16.8.4117 · DOI
10.1126/science.275.5300.665 · DOI
10.1074/jbc.272.13.8474 · DOI
10.1074/jbc.273.19.11630 · DOI
10.1073/pnas.93.15.7639 · DOI
10.1016/S0014-5793(97)00541-3 · DOI
10.1074/jbc.272.12.7713 · DOI
10.1002/j.1460-2075.1996.tb01045.x · DOI
10.1073/pnas.95.19.11211 · DOI
10.1016/S0145-2126(97)00055-6 · DOI
10.1073/pnas.94.8.3627 · DOI
10.1074/jbc.271.36.21920 · DOI
10.1074/jbc.272.50.31515 · DOI · Paper page
10.1042/0264-6021:3370575 · DOI
10.1016/S0959-437X(98)80062-2 · DOI
10.1128/MCB.19.3.1661 · DOI
10.1016/S0962-8924(97)01027-1 · DOI
10.1093/emboj/16.10.2783 · DOI
10.1128/MCB.17.8.4406 · DOI
10.1083/jcb.142.2.573 · DOI
10.1016/S0960-9822(07)00559-3 · DOI
10.1016/S0959-437X(98)80061-0 · DOI
10.1101/gad.11.18.2295 · DOI
10.1074/jbc.273.30.19080 · DOI
10.1016/S0014-5793(97)00518-8 · DOI
10.1016/S0092-8674(00)81469-5 · DOI · Paper page
10.1128/MCB.15.4.2304 · DOI
10.1038/383181a0 · DOI
10.1074/jbc.273.51.33922 · DOI · Paper page
10.1093/emboj/17.24.7294 · DOI
10.1128/MCB.18.9.5457 · DOI · Paper page
10.1074/jbc.273.26.16568 · DOI
10.1101/gad.12.13.1941 · DOI
10.1016/S0014-5793(97)00518-8 · DOI
10.1042/bj3360241 · DOI
10.1038/25147 · DOI
Ahmed NN, 1993, Oncogene, 8, 1957
10.1046/j.1432-1327.1998.2510195.x · DOI
10.1042/bj3310299 · DOI
Turinsky J, 1999, Am. J. Physiol., 276, R277
10.1074/jbc.273.13.7201 · DOI
10.1016/S0960-9822(98)70274-X · DOI
10.1016/S0092-8674(00)81092-2 · DOI
10.1016/S0014-5793(97)00323-2 · DOI
10.1023/A:1006823109415 · DOI
10.1038/370071a0 · DOI
10.1038/358070a0 · DOI
10.1073/pnas.92.25.11696 · DOI
10.1128/MCB.16.11.6242 · DOI

200 of 324 shown

Sorted by citations

Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
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
Neurotrophin signal transduction in the nervous system
Kaplan, D. R., & Miller, F. D. (2000) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00092-1 · Cited by 1,944
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
Akt Signaling Pathway in Macrophage Activation and M1/M2 Polarization
Vergadi, E., Ieronymaki, E., Lyroni, K., Vaporidi, K., & Tsatsanis, C. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601515 · Cited by 1,148
AKT plays a central role in tumorigenesis
Testa, J. R., & Bellacosa, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211430998 · Cited by 944
PTEN: The down side of PI 3-kinase signalling
Leslie, N. R., & Downes, C. P. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00234-0 · Cited by 415
Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor.
Lin, H.-K., Yeh, S., Kang, H.-Y., & Chang, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121173298 · Cited by 401
Akt provides the CD28 costimulatory signal for up-regulation of IL-2 and IFN-γ but not TH2 cytokines
Kane, L. P., Andres, P. G., Howland, K. C., Abbas, A. K., & Weiss, A. (2001) · Nature Immunology · doi:10.1038/83144 · Cited by 316
Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation
Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294
Integration of biochemical signalling in spines
Kennedy, M. B., Beale, H. C., Carlisle, H. J., & Washburn, L. R. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1685 · Cited by 286
Leptin signalling
Sweeney, G. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00006-2 · Cited by 271
Insulin Receptor Substrate-1 and Phosphoinositide-Dependent Kinase-1 Are Required for Insulin-Stimulated Production of Nitric Oxide in Endothelial Cells
Montagnani, M., Ravichandran, L. V., Chen, H., Esposito, D. L., & Quon, M. J. (2002) · Molecular Endocrinology · doi:10.1210/me.2002-0074 · Cited by 235
Akt Phosphorylates and Regulates Pdcd4 Tumor Suppressor Protein
Palamarchuk, A., Efanov, A., Maximov, V., Aqeilan, R. I., Croce, C. M., & Pekarsky, Y. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-3469 · Cited by 151
Running exercise-induced up-regulation of hippocampal brain-derived neurotrophic factor is CREB-dependent
Chen, M. J., & Russo‐Neustadt, A. A. (2009) · Hippocampus · doi:10.1002/hipo.20579 · Cited by 129
Clk2 and B56β mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt
Rodgers, J. T., Vogel, R. O., & Puigserver, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.007 · Cited by 99
Molecular and cellular aspects of age-related cognitive decline and Alzheimer’s disease
Hullinger, R., & Puglielli, L. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.05.008 · Cited by 68
Heparanase, cell signaling, and viral infections
Koganti, R., Suryawanshi, R., & Shukla, D. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03559-y · Cited by 67
IgA Fc receptor (FcαR) cross-linking recruits tyrosine kinases, phosphoinositide kinases and serine/threonine kinases to glycolipid rafts
LANG, M. L., CHEN, Y.-W., SHEN, L., GAO, H., LANG, G. A., WADE, T. K., & WADE, W. F. (2002) · Biochemical Journal · doi:10.1042/bj20011696 · Cited by 60
AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain
Rieske, P., & Pongubala, J. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007482200 · Cited by 54
Expression of the β3 subunit of Na+/K+-ATPase is increased in gastric cancer and regulates gastric cancer cell progression and prognosis via the PI3/AKT pathway
Li, L., Feng, R., Xu, Q., Zhang, F., Liu, T., Cao, J., & Fei, S. (2017) · Oncotarget · doi:10.18632/oncotarget.20894 · Cited by 41
PH domain-mediated autoinhibition and oncogenic activation of Akt
Bae, H., Viennet, T., Park, E., Chu, N., Salguero, A., Eck, M. J., Arthanari, H., & Cole, P. A. (2022) · eLife · doi:10.7554/elife.80148 · Cited by 31
An OX-Tra’Ordinary tale: the role of OX40 and OX40L in atopic dermatitis
Sadrolashrafi, K., Guo, L., Kikuchi, R., Hao, A., Yamamoto, R. K., Tolson, H. C., Bilimoria, S. N., Yee, D. K., & Armstrong, A. W. (2024) · Cells · doi:10.3390/cells13070587 · Cited by 28

Authors: Chan, T. O., Rittenhouse, S. E., & Tsichlis, P. N.
Affiliations: Kimmel Cancer Institute, Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107;
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 1999-06
Volume: 68
Issue: 1
Pages: 965-1014
ISSN: 0066-4154
1545-4509
DOI: 10.1146/annurev.biochem.68.1.965
Cited by: 737
References: 12
Language: en

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

AKT/PKB and Other D3 Phosphoinositide-Regulated Kinases: Kinase Activation by Phosphoinositide-Dependent Phosphorylation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks