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Molecular cloning and characterization of a new member of the RAC protein kinase family: Association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and beta gamma subunits of G proteins
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Konishi H, Kuroda S, Tanaka M, Matsuzaki H, Ono Y, Kameyama K, Haga T, Kikkawa U. Molecular cloning and characterization of a new member of the RAC protein kinase family: association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and beta gamma subunits of G proteins. Biochem Biophys Res Commun. 216:1995;526-534.
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The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
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Franke TF, Yang S-I, Chan TO, Datta K, Kazlauskas A, Morrison DK, Kaplan DR, Tsichlis PN. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 81:1995;727-736.
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Kohn AD, Kovacina KS, Roth RA. Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase. EMBO J. 14:1995;4288-4295.
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Kohn, A.D.1
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Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal transducing kinase pathways
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Klippel A, Reinhard C, Kavanaugh WM, Apell G, Escobedo MA, Williams LT. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal transducing kinase pathways. Mol Cell Biol. 16:1996;4117-4127.
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Klippel, A.1
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PI3K and PKB/Akt act as an effector pathway for R-Ras
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Marte BM, Rodriguez-Viciana P, Wennstrsm S, Warne PH, Downward J. PI3K and PKB/Akt act as an effector pathway for R-Ras. Curr Biol. 7:1997;63-70.
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Marte, B.M.1
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Downward, J.5
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11
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0031039024
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Direct regulation of the akt protooncogene product by phosphatidylinositol-3,4-bisphosphate
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2. PI(3,4)P2 is shown to activate the kinase activity of PKB/Akt, at least weakly, in vitro.
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2. PI(3,4)P2 is shown to activate the kinase activity of PKB/Akt, at least weakly, in vitro.
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Science
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Franke, T.F.1
Kaplan, D.R.2
Cantley, L.C.3
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12
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0030265564
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Constitutive activation of protein-kinase-b and phosphorylation of p47(phox) by membrane-targeted phosphoinositide 3-kinase
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Didichenko SA, Tilton B, Hemmings BA, Ballmerhofer K, Thelen M. Constitutive activation of protein-kinase-b and phosphorylation of p47(phox) by membrane-targeted phosphoinositide 3-kinase. Curr Biol. 6:1996;1271-1278.
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13
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0028074316
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Phosphatidylinositol-3-OH kinase as a direct target of Ras
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Rodriguez-Viciana P, Warne PH, Dhand R, Vanhaesebroeck B, Gout I, Fry MJ, Waterfield MD, Downward J. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature. 370:1994;527-532.
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14
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Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation
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Rodriguez-Viciana P, Warne PH, Vanhaesebroeck B, Waterfield MD, Downward J. Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. EMBO J. 15:1996;2442-2451.
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Rodriguez-Viciana, P.1
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Waterfield, M.D.4
Downward, J.5
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15
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0029807471
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Akt is a direct target of the phosphatidylinositol 3-kinase - activation by growth-factors, v-src and v-ha-ras, in Sf9 and mammalian-cells
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Datta K, Bellacosa A, Chan TO, Tsichlis PN. Akt is a direct target of the phosphatidylinositol 3-kinase - activation by growth-factors, v-src and v-ha-ras, in Sf9 and mammalian-cells. J Biol Chem. 271:1996;30835-30839.
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Datta, K.1
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Tsichlis, P.N.4
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16
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0030913673
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Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
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of outstanding interest. Adhesion of epithelial cells to matrix is shown to activate PKB/Akt and protect them from apoptosis. In addition, PKB/Akt is shown to be the pathway used by oncogenic Ras to protect epithelial cells from apoptosis induced by membrane detachment.
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Khwaja A, Rodriguez-Viciana P, Wennstrom S, Warne PH, Downward J. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. of outstanding interest EMBO J. 16:1997;2783-2793 Adhesion of epithelial cells to matrix is shown to activate PKB/Akt and protect them from apoptosis. In addition, PKB/Akt is shown to be the pathway used by oncogenic Ras to protect epithelial cells from apoptosis induced by membrane detachment.
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EMBO J
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Khwaja, A.1
Rodriguez-Viciana, P.2
Wennstrom, S.3
Warne, P.H.4
Downward, J.5
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17
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0030839766
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Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation
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of special interest. Adhesion of epithelial cells to matrix activates PKB/Akt.
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King WG, Mattaliano MD, Chan TO, Tsichlis PN, Brugge JS. Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation. of special interest Mol Cell Biol. 17:1997;4406-4418 Adhesion of epithelial cells to matrix activates PKB/Akt.
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Mol Cell Biol
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King, W.G.1
Mattaliano, M.D.2
Chan, T.O.3
Tsichlis, P.N.4
Brugge, J.S.5
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18
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0029821721
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Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase
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Konishi H, Matsuzaki H, Tanaka M, Ono Y, Tokunaga C, Kuroda S, Kikkawa U. Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA. 93:1996;7639-7643.
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Konishi, H.1
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Tanaka, M.3
Ono, Y.4
Tokunaga, C.5
Kuroda, S.6
Kikkawa, U.7
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19
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0027985080
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Molecular cloning of rat RAC protein kinase alpha and beta and their association with protein kinase C zeta
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Konishi H, Shinomura T, Kuroda S, Ono Y, Kikkawa U. Molecular cloning of rat RAC protein kinase alpha and beta and their association with protein kinase C zeta. Biochem Biophys Res Commun. 205:1994;817-825.
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Konishi, H.1
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Ono, Y.4
Kikkawa, U.5
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20
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0029942186
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Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors
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Andjelkovic M, Jakubowicz T, Cron P, Ming XF, Han JW, Hemmings BA. Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc Natl Acad Sci USA. 93:1996;5699-5704.
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Andjelkovic, M.1
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Cron, P.3
Ming, X.F.4
Han, J.W.5
Hemmings, B.A.6
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21
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0029993517
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Specific binding of Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
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2. In this case, lipid binding does not stimulate the kinase activity of PKB/Akt. (Compare Franke, 1997 [11], Klippel, 1997 [22], Frech, 1997 [23].)
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2. In this case, lipid binding does not stimulate the kinase activity of PKB/Akt. (Compare Franke, 1997 [11], Klippel, 1997 [22], Frech, 1997 [23].).
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Biochem J
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James, S.R.1
Downes, C.P.2
Gigg, R.3
Grove, S.J.A.4
Holmes, A.B.5
Alessi, D.R.6
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22
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0031015986
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A specific product of phosphatidylinositol 3-kinase directly activates the protein-kinase akt through its pleckstrin homology domain
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2 stimulating the kinase activity of PKB/Akt moderately.
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2 stimulating the kinase activity of PKB/Akt moderately.
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Mol Cell Biol
, vol.17
, pp. 338-344
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Klippel, A.1
Kavanaugh, W.M.2
Pot, D.3
Williams, L.T.4
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24
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15644381754
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Role of translocation in the activation and function of protein kinase B
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of outstanding interest. A detailed and conclusive study showing that PKB/Akt translocates to the plasma membrane, and eventually to the nucleus, following growth factor stimulation of cells. Membrane translocation is shown to be sufficient to cause phosphorylation of regulatory sites on PKB/Akt by upstream kinases.
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Andjelkovic M, Alessi DR, Meier R, Fernandez A, Lamb NJC, Frech M, Cron P, Lucocq JM, Hemmings BA. Role of translocation in the activation and function of protein kinase B. of outstanding interest J Biol Chem. 272:1997;31515-31524 A detailed and conclusive study showing that PKB/Akt translocates to the plasma membrane, and eventually to the nucleus, following growth factor stimulation of cells. Membrane translocation is shown to be sufficient to cause phosphorylation of regulatory sites on PKB/Akt by upstream kinases.
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(1997)
J Biol Chem
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Andjelkovic, M.1
Alessi, D.R.2
Meier, R.3
Fernandez, A.4
Lamb, N.J.C.5
Frech, M.6
Cron, P.7
Lucocq, J.M.8
Hemmings, B.A.9
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25
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0029804116
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Mechanism of activation of protein kinase B by insulin and IGF-1
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of outstanding interest. The identification of the sites phosphorylated on PKB/Akt in response to insulin treatment: threonine 308 and serine 473.
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Alessi DR, Andjelkovic M, Caudwell B, Cron P, Morrice N, Cohen P, Hemmings BA. Mechanism of activation of protein kinase B by insulin and IGF-1. of outstanding interest EMBO J. 15:1996;6541-6551 The identification of the sites phosphorylated on PKB/Akt in response to insulin treatment: threonine 308 and serine 473.
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EMBO J
, vol.15
, pp. 6541-6551
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Alessi, D.R.1
Andjelkovic, M.2
Caudwell, B.3
Cron, P.4
Morrice, N.5
Cohen, P.6
Hemmings, B.A.7
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26
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0029810181
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Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation
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Kohn AD, Takeuchi F, Roth RA. Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J Biol Chem. 271:1996;21920-21926.
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J Biol Chem
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Kohn, A.D.1
Takeuchi, F.2
Roth, R.A.3
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27
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0031127305
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Purification and characterisation of a phosphatidylinositol 3,4,5 trisphosphate dependent protein kinase (PDK1) that phosphorylates and activates protein kinase Bα
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2.
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2.
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(1997)
Curr Biol
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Alessi, D.R.1
James, S.R.2
Downes, C.P.3
Holmes, A.B.4
Gaffney, P.5
Reece, C.6
Cohen, P.7
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28
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0030799706
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Dual role of phosphatidylinositol-3,4,5-triphosphate in the activation of protein kinase B
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of outstanding interest. See Alessi, James, 1997 [27].
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Stokoe D, Stephens LR, Copeland T, Gaffney PR, Reese CB, Painter GF, Holmes AB, McCormick K, Hawkins PT. Dual role of phosphatidylinositol-3,4,5-triphosphate in the activation of protein kinase B. of outstanding interest Science. 277:1997;567-570 See Alessi, James, 1997 [27].
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Science
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Stokoe, D.1
Stephens, L.R.2
Copeland, T.3
Gaffney, P.R.4
Reese, C.B.5
Painter, G.F.6
Holmes, A.B.7
McCormick, K.8
Hawkins, P.T.9
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29
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12644301164
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3-phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase
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of outstanding interest. The report of the cloning of PDK1. The kinase has a PH domain at its carboxyl terminus and is from the same family as PKB/Akt itself.
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Alessi DR, Deak M, Casamayor A, Caudwell FB, Morrice N, Norman DG, Gaffney D, Reese CB, MacDougall CN, Harbison D, et al. 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. of outstanding interest Curr Biol. 7:1997;776-789 The report of the cloning of PDK1. The kinase has a PH domain at its carboxyl terminus and is from the same family as PKB/Akt itself.
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Curr Biol
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Alessi, D.R.1
Deak, M.2
Casamayor, A.3
Caudwell, F.B.4
Morrice, N.5
Norman, D.G.6
Gaffney, D.7
Reese, C.B.8
MacDougall, C.N.9
Harbison, D.10
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30
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0030590875
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Molecular basis for the substrate specificity of protein kinase B; Comparison with MAPKAP kinase-1 and p70 S6 kinase
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Alessi DR, Caudwell FB, Andjelkovic M, Hemmings BA, Cohen P. Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett. 399:1996;333-338.
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FEBS Lett
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Alessi, D.R.1
Caudwell, F.B.2
Andjelkovic, M.3
Hemmings, B.A.4
Cohen, P.5
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0029587224
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Inhibition of glycogen synthase kinase-3 by insulin mediated protein kinase B
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Cross DAE, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated protein kinase B. Nature. 378:1995;785-789.
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Nature
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Cross, D.A.E.1
Alessi, D.R.2
Cohen, P.3
Andjelkovich, M.4
Hemmings, B.A.5
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0030712317
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Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216
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Shaw M, Cohen P, Alessi DR. Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216. FEBS Lett. 416:1997;307-311.
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FEBS Lett
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Shaw, M.1
Cohen, P.2
Alessi, D.R.3
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0030748651
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Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
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of special interest. Identification of another metabolic enzyme which is a direct substrate for PKB/Akt, providing further insight into how PKB/Akt contributes to the effects of insulin on cellular metabolism.
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Deprez J, Vertommen D, Alessi DR, Hue L, Rider MH. Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades. of special interest J Biol Chem. 272:1997;17269-17275 Identification of another metabolic enzyme which is a direct substrate for PKB/Akt, providing further insight into how PKB/Akt contributes to the effects of insulin on cellular metabolism.
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J Biol Chem
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Deprez, J.1
Vertommen, D.2
Alessi, D.R.3
Hue, L.4
Rider, M.H.5
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35
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0029908016
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Expression of a constitutively active Akt ser/thr kinase in 3T3-I1 adipocytes stimulates glucose-uptake and glucose-transporter-4 translocation
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Kohn AD, Summers SA, Birnbaum MJ, Roth RA. Expression of a constitutively active Akt ser/thr kinase in 3T3-I1 adipocytes stimulates glucose-uptake and glucose-transporter-4 translocation. J Biol Chem. 271:1996;31372-31378.
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J Biol Chem
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Kohn, A.D.1
Summers, S.A.2
Birnbaum, M.J.3
Roth, R.A.4
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36
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0029891232
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Expression of a constitutively activated form of protein-kinase-β (c-akt) in 3T3-I1 preadipose cells causes spontaneous differentiation
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Magun R, Burgering BMT, Coffer PJ, Pardasani D, Lin Y, Chabot J, Sorisky A. Expression of a constitutively activated form of protein-kinase-β (c-akt) in 3T3-I1 preadipose cells causes spontaneous differentiation. Endocrinology. 137:1996;3590-3593.
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Endocrinology
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Magun, R.1
Burgering, B.M.T.2
Coffer, P.J.3
Pardasani, D.4
Lin, Y.5
Chabot, J.6
Sorisky, A.7
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37
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0028963084
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Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
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Yao RJ, Cooper GM. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science. 267:1995;2003-2006.
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Science
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Yao, R.J.1
Cooper, G.M.2
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0029834691
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Growth factor-dependent survival of rodent fibroblasts requires phosphatidylinositol 3-kinase but is independent of pp70S6K activity
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Yao R, Cooper GM. Growth factor-dependent survival of rodent fibroblasts requires phosphatidylinositol 3-kinase but is independent of pp70S6K activity. Oncogene. 13:1996;343-351.
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Oncogene
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Yao, R.1
Cooper, G.M.2
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39
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0031034574
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Anti-apoptotic signalling by the IGF-I receptor, PI3K and Akt
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of special interest. PKB/Akt protects epithelial cells from radiation-induced apoptosis.
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Kulik G, Klippel A, Weber MJ. Anti-apoptotic signalling by the IGF-I receptor, PI3K and Akt. of special interest Mol Cell Biol. 17:1997;1595-1606 PKB/Akt protects epithelial cells from radiation-induced apoptosis.
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Mol Cell Biol
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, pp. 1595-1606
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Kulik, G.1
Klippel, A.2
Weber, M.J.3
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40
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0031053586
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Regulation of neuronal survival by the serine-threonine protein kinase Akt
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of special interest. PKB/Akt mediates IGF-1 protection of neuronal cells from apoptosis.
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Dudek H, Datta SR, Franke TF, Birnbaum MJ, Yao RJ, Cooper GM, Segal RA, Kaplan DR, Greenberg ME. Regulation of neuronal survival by the serine-threonine protein kinase Akt. of special interest Science. 275:1997;661-665 PKB/Akt mediates IGF-1 protection of neuronal cells from apoptosis.
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Science
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Dudek, H.1
Datta, S.R.2
Franke, T.F.3
Birnbaum, M.J.4
Yao, R.J.5
Cooper, G.M.6
Segal, R.A.7
Kaplan, D.R.8
Greenberg, M.E.9
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41
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0030694175
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The PI3K/akt signaling pathway delivers an anti-apoptotic signal
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of special interest. PKB/Akt protects fibroblasts from apoptosis caused by expression of c-myc in the absence of serum.
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Kennedy SG, Wagner AJ, Conzen SD, Jordan J, Bellacosa A, Tsichlis PN, Hay N. The PI3K/akt signaling pathway delivers an anti-apoptotic signal. of special interest Genes Dev. 11:1997;701-713 PKB/Akt protects fibroblasts from apoptosis caused by expression of c-myc in the absence of serum.
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Suppression of c-myc-induced apoptosis by Ras signaling through PI(3)K and PKB
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of special interest. The effect of activated Ras on fibroblast survival in the absence of serum with forced Myc expression is shown to be the sum of a death-inducing signal mediated by the Raf - MAP kinase pathway and a survival signal mediated by PI 3-kinase and PKB/Akt.
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45
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46
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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
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L/Bcl-2 binding ability and death-promoting function. This provides a possible link between PKB/Akt and apoptosis regulation; however, it should be noted that these experiments used overexpressed BAD and that many cells do not normally express BAD.
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L/Bcl-2 binding ability and death-promoting function. This provides a possible link between PKB/Akt and apoptosis regulation; however, it should be noted that these experiments used overexpressed BAD and that many cells do not normally express BAD.
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