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Volumn 1784, Issue 1, 2008, Pages 159-185

Targeting phosphoinositide 3-kinase-Moving towards therapy

Author keywords

Allergy; Cancer; Drug development; Inflammation; Pharmacology; PI3K

Indexed keywords

2 (6 AMINO 9 PURINYLMETHYL) 5 METHYL 3 (2 METHYLPHENYL) 3H QUINAZOLIN 4 ONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 5 [5 (4 FLUORO 2 HYDROXYPHENYL)FURFURYLIDENE] 2,4 THIAZOLIDINEDIONE; 9 (1 ANILINOETHYL) 7 METHYL 2 MORPHOLINOPYRIDO[1,2 A]PYRIMIDIN 4 ONE; AS 604850; BAY 247; D 030; DNA DEPENDENT PROTEIN KINASE; GENE PRODUCT; GROWTH FACTOR RECEPTOR; KU 55399; LIPHAGAL; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE GAMMA; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PIK 239; PIK 294; PIK 39; PIK 90; PROTEIN KINASE B; PROTEIN SERINE THREONINE KINASE; PROTEIN TEP1; PX 866; TARGET OF RAPAMYCIN KINASE; TGX 286; TUBERIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; WORTMANNIN; XL 147; XL 765;

EID: 38149120449     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.10.003     Document Type: Review
Times cited : (522)

References (266)
  • 1
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman M., Kaplan D.R., Schaffhausen B., Cantley L., and Roberts T.M. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315 (1985) 239-242
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 2
    • 0011168670 scopus 로고
    • Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol
    • Sugimoto Y., Whitman M., Cantley L.C., and Erikson R.L. Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 2117-2121
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 2117-2121
    • Sugimoto, Y.1    Whitman, M.2    Cantley, L.C.3    Erikson, R.L.4
  • 3
    • 0021221071 scopus 로고
    • Transforming protein of avian sarcoma virus UR2 is associated with phosphatidylinositol kinase activity: possible role in tumorigenesis
    • Macara I.G., Marinetti G.V., and Balduzzi P.C. Transforming protein of avian sarcoma virus UR2 is associated with phosphatidylinositol kinase activity: possible role in tumorigenesis. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 2728-2732
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 2728-2732
    • Macara, I.G.1    Marinetti, G.V.2    Balduzzi, P.C.3
  • 4
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • Cully M., You H., Levine A.J., and Mak T.W. Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis. Nat. Rev., Cancer 6 (2006) 184-192
    • (2006) Nat. Rev., Cancer , vol.6 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 5
    • 15044338824 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in disease: timing, location, and scaffolding
    • Wymann M.P., and Marone R. Phosphoinositide 3-kinase in disease: timing, location, and scaffolding. Curr. Opin. Cell Biol. 17 (2005) 141-149
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 141-149
    • Wymann, M.P.1    Marone, R.2
  • 6
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I., and Sawyers C.L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat. Rev., Cancer 2 (2002) 489-501
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 7
    • 0029612196 scopus 로고
    • A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction
    • MacDougall L.K., Domin J., and Waterfield M.D. A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction. Curr. Biol. 5 (1995) 1404-1415
    • (1995) Curr. Biol. , vol.5 , pp. 1404-1415
    • MacDougall, L.K.1    Domin, J.2    Waterfield, M.D.3
  • 9
    • 0029768753 scopus 로고    scopus 로고
    • A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans
    • Morris J.Z., Tissenbaum H.A., and Ruvkun G. A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans. Nature 382 (1996) 536-539
    • (1996) Nature , vol.382 , pp. 536-539
    • Morris, J.Z.1    Tissenbaum, H.A.2    Ruvkun, G.3
  • 10
    • 0037007215 scopus 로고    scopus 로고
    • Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane
    • Roggo L., Bernard V., Kovacs A.L., Rose A.M., Savoy F., Zetka M., Wymann M.P., and Muller F. Membrane transport in Caenorhabditis elegans: an essential role for VPS34 at the nuclear membrane. EMBO J. 21 (2002) 1673-1683
    • (2002) EMBO J. , vol.21 , pp. 1673-1683
    • Roggo, L.1    Bernard, V.2    Kovacs, A.L.3    Rose, A.M.4    Savoy, F.5    Zetka, M.6    Wymann, M.P.7    Muller, F.8
  • 12
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu P.V., Takegawa K., Fry M.J., Stack J.H., Waterfield M.D., and Emr S.D. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260 (1993) 88-91
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 13
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman J.A., Luo J., and Cantley L.C. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev., Genet. 7 (2006) 606-619
    • (2006) Nat. Rev., Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 14
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann M.P., and Pirola L. Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1436 (1998) 127-150
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 16
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 296 (2002) 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 17
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system?
    • Stephens L.R., Jackson T.R., and Hawkins P.T. Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system?. Biochim. Biophys. Acta 1179 (1993) 27-75
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 27-75
    • Stephens, L.R.1    Jackson, T.R.2    Hawkins, P.T.3
  • 18
    • 0042734621 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signaling-Which way to target?
    • Wymann M.P., Zvelebil M., and Laffargue M. Phosphoinositide 3-kinase signaling-Which way to target?. Trends Pharmacol. Sci. 24 (2003) 366-376
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 366-376
    • Wymann, M.P.1    Zvelebil, M.2    Laffargue, M.3
  • 19
    • 34247141906 scopus 로고    scopus 로고
    • Role of class II phosphoinositide 3-kinase in cell signaling
    • Falasca M., and Maffucci T. Role of class II phosphoinositide 3-kinase in cell signaling. Biochem. Soc. Trans. 35 (2007) 211-214
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 211-214
    • Falasca, M.1    Maffucci, T.2
  • 20
    • 0034697119 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
    • Domin J., Gaidarov I., Smith M.E., Keen J.H., and Waterfield M.D. The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles. J. Biol. Chem. 275 (2000) 11943-11950
    • (2000) J. Biol. Chem. , vol.275 , pp. 11943-11950
    • Domin, J.1    Gaidarov, I.2    Smith, M.E.3    Keen, J.H.4    Waterfield, M.D.5
  • 21
    • 0035103107 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking
    • Gaidarov I., Smith M.E., Domin J., and Keen J.H. The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol. Cell 7 (2001) 443-449
    • (2001) Mol. Cell , vol.7 , pp. 443-449
    • Gaidarov, I.1    Smith, M.E.2    Domin, J.3    Keen, J.H.4
  • 22
    • 22344452002 scopus 로고    scopus 로고
    • Class II phosphoinositide 3-kinase defines a novel signaling pathway in cell migration
    • Maffucci T., Cooke F.T., Foster F.M., Traer C.J., Fry M.J., and Falasca M. Class II phosphoinositide 3-kinase defines a novel signaling pathway in cell migration. J. Cell Biol. 169 (2005) 789-799
    • (2005) J. Cell Biol. , vol.169 , pp. 789-799
    • Maffucci, T.1    Cooke, F.T.2    Foster, F.M.3    Traer, C.J.4    Fry, M.J.5    Falasca, M.6
  • 23
    • 0026564092 scopus 로고
    • An essential role for a protein and lipid kinase complex in secretory protein sorting
    • Herman P.K., Stack J.H., and Emr S.D. An essential role for a protein and lipid kinase complex in secretory protein sorting. Trends Cell Biol. 2 (1992) 363-368
    • (1992) Trends Cell Biol. , vol.2 , pp. 363-368
    • Herman, P.K.1    Stack, J.H.2    Emr, S.D.3
  • 24
  • 26
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara A., Noda T., Ishihara N., and Ohsumi Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152 (2001) 519-530
    • (2001) J. Cell Biol. , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 27
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A., Kabeya Y., Ohsumi Y., and Yoshimori T. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2 (2001) 330-335
    • (2001) EMBO Rep. , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 29
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue Z., Jin S., Yang C., Levine A.J., and Heintz N. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 15077-15082
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 30
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann S.G., and Thomas G. The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett. 580 (2006) 2821-2829
    • (2006) FEBS Lett. , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 31
    • 34247120977 scopus 로고    scopus 로고
    • Nutrient sensing in the mTOR/S6K1 signalling pathway
    • Gulati P., and Thomas G. Nutrient sensing in the mTOR/S6K1 signalling pathway. Biochem. Soc. Trans. 35 (2007) 236-238
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 236-238
    • Gulati, P.1    Thomas, G.2
  • 32
    • 33847743064 scopus 로고    scopus 로고
    • hvps34, an ancient player, enters a growing game: mTOR Complex1/S6K1 signaling
    • Nobukuni T., Kozma S.C., and Thomas G. hvps34, an ancient player, enters a growing game: mTOR Complex1/S6K1 signaling. Curr. Opin. Cell Biol. 19 (2007) 135-141
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 135-141
    • Nobukuni, T.1    Kozma, S.C.2    Thomas, G.3
  • 33
    • 33745933535 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases: old enzymes with emerging functions
    • Balla A., and Balla T. Phosphatidylinositol 4-kinases: old enzymes with emerging functions. Trends Cell Biol. 16 (2006) 351-361
    • (2006) Trends Cell Biol. , vol.16 , pp. 351-361
    • Balla, A.1    Balla, T.2
  • 34
    • 0037205494 scopus 로고    scopus 로고
    • Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments
    • Balla A., Tuymetova G., Barshishat M., Geiszt M., and Balla T. Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments. J. Biol. Chem. 277 (2002) 20041-20050
    • (2002) J. Biol. Chem. , vol.277 , pp. 20041-20050
    • Balla, A.1    Tuymetova, G.2    Barshishat, M.3    Geiszt, M.4    Balla, T.5
  • 36
    • 0030989280 scopus 로고    scopus 로고
    • Subcellular locations of phosphatidylinositol 4-kinase isoforms
    • Wong K., Meyers D., and Cantley L.C. Subcellular locations of phosphatidylinositol 4-kinase isoforms. J. Biol. Chem. 272 (1997) 13236-13241
    • (1997) J. Biol. Chem. , vol.272 , pp. 13236-13241
    • Wong, K.1    Meyers, D.2    Cantley, L.C.3
  • 37
    • 0033807922 scopus 로고    scopus 로고
    • Immunohistochemical localisation of two phosphatidylinositol 4-kinase isoforms, PI4K230 and PI4K92, in the central nervous system of rats
    • Balla A., Vereb G., Gulkan H., Gehrmann T., Gergely P., Heilmeyer L.M.J., and Antal M. Immunohistochemical localisation of two phosphatidylinositol 4-kinase isoforms, PI4K230 and PI4K92, in the central nervous system of rats. Exp. Brain Res. 134 (2000) 279-288
    • (2000) Exp. Brain Res. , vol.134 , pp. 279-288
    • Balla, A.1    Vereb, G.2    Gulkan, H.3    Gehrmann, T.4    Gergely, P.5    Heilmeyer, L.M.J.6    Antal, M.7
  • 38
    • 0034120471 scopus 로고    scopus 로고
    • Localization of two distinct type III phosphatidylinositol 4-kinase enzyme mRNAs in the rat
    • Zolyomi A., Zhao X., Downing G.J., and Balla T. Localization of two distinct type III phosphatidylinositol 4-kinase enzyme mRNAs in the rat. Am. J. Physiol., Cell Physiol. 278 (2000) C914-C920
    • (2000) Am. J. Physiol., Cell Physiol. , vol.278
    • Zolyomi, A.1    Zhao, X.2    Downing, G.J.3    Balla, T.4
  • 39
    • 0035890154 scopus 로고    scopus 로고
    • Proteomic and functional evidence for a P2X7 receptor signalling complex
    • Kim M., Jiang L.H., Wilson H.L., North R.A., and Surprenant A. Proteomic and functional evidence for a P2X7 receptor signalling complex. EMBO J. 20 (2001) 6347-6358
    • (2001) EMBO J. , vol.20 , pp. 6347-6358
    • Kim, M.1    Jiang, L.H.2    Wilson, H.L.3    North, R.A.4    Surprenant, A.5
  • 41
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: safeguarding genome integrity
    • Shiloh Y. ATM and related protein kinases: safeguarding genome integrity. Nat. Rev., Cancer 3 (2003) 155-168
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 42
    • 3242882820 scopus 로고    scopus 로고
    • PI 3-kinase related kinases: 'big' players in stress-induced signaling pathways
    • Abraham R.T. PI 3-kinase related kinases: 'big' players in stress-induced signaling pathways. DNA Repair (Amst.) 3 (2004) 883-887
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 883-887
    • Abraham, R.T.1
  • 43
    • 0035313706 scopus 로고    scopus 로고
    • DNA-PK, ATM and ATR as sensors of DNA damage: variations on a theme?
    • Durocher D., and Jackson S.P. DNA-PK, ATM and ATR as sensors of DNA damage: variations on a theme?. Curr. Opin. Cell Biol. 13 (2001) 225-231
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 225-231
    • Durocher, D.1    Jackson, S.P.2
  • 44
    • 20544441070 scopus 로고    scopus 로고
    • DNA repair: how to PIKK a partner
    • Hiom K. DNA repair: how to PIKK a partner. Curr. Biol. 15 (2005) R473-R475
    • (2005) Curr. Biol. , vol.15
    • Hiom, K.1
  • 45
    • 29144507015 scopus 로고    scopus 로고
    • The role of SMG-1 in nonsense-mediated mRNA decay
    • Yamashita A., Kashima I., and Ohno S. The role of SMG-1 in nonsense-mediated mRNA decay. Biochim. Biophys. Acta 1754 (2005) 305-315
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 305-315
    • Yamashita, A.1    Kashima, I.2    Ohno, S.3
  • 46
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., and Hall M.N. TOR signaling in growth and metabolism. Cell 124 (2006) 471-484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 48
    • 33748934979 scopus 로고    scopus 로고
    • mTORC2 caught in a SINful Akt
    • Polak P., and Hall M.N. mTORC2 caught in a SINful Akt. Dev. Cell 11 (2006) 433-434
    • (2006) Dev. Cell , vol.11 , pp. 433-434
    • Polak, P.1    Hall, M.N.2
  • 49
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning B.D., and Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 129 (2007) 1261-1274
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 50
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng J., Park J., Cron P., Hess D., and Hemmings B.A. Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279 (2004) 41189-41196
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 51
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT-A major therapeutic target
    • Hanada M., Feng J., and Hemmings B.A. Structure, regulation and function of PKB/AKT-A major therapeutic target. Biochim. Biophys. Acta 1697 (2004) 3-16
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 52
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil D.P., Park J., and Hemmings B.A. PKB binding proteins. Getting in on the Akt. Cell 111 (2002) 293-303
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 53
    • 0034733569 scopus 로고    scopus 로고
    • The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase
    • Kisseleva M.V., Wilson M.P., and Majerus P.W. The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase. J. Biol. Chem. 275 (2000) 20110-20116
    • (2000) J. Biol. Chem. , vol.275 , pp. 20110-20116
    • Kisseleva, M.V.1    Wilson, M.P.2    Majerus, P.W.3
  • 57
    • 0036629251 scopus 로고    scopus 로고
    • Cell cycle and death control: long live forkheads
    • Burgering B.M., and Kops G.J. Cell cycle and death control: long live forkheads. Trends Biochem. Sci. 27 (2002) 352-360
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 352-360
    • Burgering, B.M.1    Kops, G.J.2
  • 58
    • 0035909313 scopus 로고    scopus 로고
    • Forkhead transcription factors contribute to execution of the mitotic programme in mammals
    • Alvarez B., Martinez-A C., Burgering B.M., and Carrera A.C. Forkhead transcription factors contribute to execution of the mitotic programme in mammals. Nature 413 (2001) 744-747
    • (2001) Nature , vol.413 , pp. 744-747
    • Alvarez, B.1    Martinez-A, C.2    Burgering, B.M.3    Carrera, A.C.4
  • 59
    • 0038003956 scopus 로고    scopus 로고
    • Decisions on life and death: FOXO forkhead transcription factors are in command when PKB/Akt is off duty
    • Burgering B.M., and Medema R.H. Decisions on life and death: FOXO forkhead transcription factors are in command when PKB/Akt is off duty. J. Leukoc. Biol. 73 (2003) 689-701
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 689-701
    • Burgering, B.M.1    Medema, R.H.2
  • 60
    • 2342618936 scopus 로고    scopus 로고
    • Multiple roles of the PI3K/PKB (Akt) pathway in cell cycle progression
    • Liang J., and Slingerland J.M. Multiple roles of the PI3K/PKB (Akt) pathway in cell cycle progression. Cell Cycle 2 (2003) 339-345
    • (2003) Cell Cycle , vol.2 , pp. 339-345
    • Liang, J.1    Slingerland, J.M.2
  • 61
    • 33746601879 scopus 로고    scopus 로고
    • Check, double check: the G2 barrier to cancer
    • Foijer F., and te Riele H. Check, double check: the G2 barrier to cancer. Cell Cycle 5 (2006) 831-836
    • (2006) Cell Cycle , vol.5 , pp. 831-836
    • Foijer, F.1    te Riele, H.2
  • 63
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L., Gonzalez-Garcia M., Page C., Herrera R., and Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278 (1997) 687-689
    • (1997) Science , vol.278 , pp. 687-689
    • del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 64
    • 0030702123 scopus 로고    scopus 로고
    • 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., and Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91 (1997) 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 65
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li Q., and Verma I.M. NF-kappaB regulation in the immune system. Nat. Rev., Immunol. 2 (2002) 725-734
    • (2002) Nat. Rev., Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 66
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes O.N., Mayo L.D., Gustin J.A., Pfeffer S.R., Pfeffer L.M., and Donner D.B. NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401 (1999) 82-85
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 67
    • 0442323560 scopus 로고    scopus 로고
    • Tuberous sclerosis complex: from Drosophila to human disease
    • Pan D., Dong J., Zhang Y., and Gao X. Tuberous sclerosis complex: from Drosophila to human disease. Trends Cell Biol. 14 (2004) 78-85
    • (2004) Trends Cell Biol. , vol.14 , pp. 78-85
    • Pan, D.1    Dong, J.2    Zhang, Y.3    Gao, X.4
  • 68
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N., and Sonenberg N. Upstream and downstream of mTOR. Genes Dev. 18 (2004) 1926-1945
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 69
    • 15044350668 scopus 로고    scopus 로고
    • The expanding TOR signaling network
    • Martin D.E., and Hall M.N. The expanding TOR signaling network. Curr. Opin. Cell Biol. 17 (2005) 158-166
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 158-166
    • Martin, D.E.1    Hall, M.N.2
  • 73
    • 0038549067 scopus 로고    scopus 로고
    • PI3K in lymphocyte development, differentiation and activation
    • Okkenhaug K., and Vanhaesebroeck B. PI3K in lymphocyte development, differentiation and activation. Nat. Rev., Immunol. 3 (2003) 317-330
    • (2003) Nat. Rev., Immunol. , vol.3 , pp. 317-330
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 74
    • 0033574429 scopus 로고    scopus 로고
    • Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110alpha subunit of phosphoinositide 3-kinase
    • Bi L., Okabe I., Bernard D.J., Wynshaw-Boris A., and Nussbaum R.L. Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110alpha subunit of phosphoinositide 3-kinase. J. Biol. Chem. 274 (1999) 10963-10968
    • (1999) J. Biol. Chem. , vol.274 , pp. 10963-10968
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Wynshaw-Boris, A.4    Nussbaum, R.L.5
  • 75
    • 0036185944 scopus 로고    scopus 로고
    • Early embryonic lethality in mice deficient in the p110beta catalytic subunit of PI 3-kinase
    • Bi L., Okabe I., Bernard D.J., and Nussbaum R.L. Early embryonic lethality in mice deficient in the p110beta catalytic subunit of PI 3-kinase. Mamm. Genome 13 (2002) 169-172
    • (2002) Mamm. Genome , vol.13 , pp. 169-172
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Nussbaum, R.L.4
  • 78
    • 0037695593 scopus 로고    scopus 로고
    • Essential, nonredundant role for the phosphoinositide 3-kinase p110delta in signaling by the B-cell receptor complex
    • Jou S.T., Carpino N., Takahashi Y., Piekorz R., Chao J.R., Carpino N., Wang D., and Ihle J.N. Essential, nonredundant role for the phosphoinositide 3-kinase p110delta in signaling by the B-cell receptor complex. Mol. Cell. Biol. 22 (2002) 8580-8591
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8580-8591
    • Jou, S.T.1    Carpino, N.2    Takahashi, Y.3    Piekorz, R.4    Chao, J.R.5    Carpino, N.6    Wang, D.7    Ihle, J.N.8
  • 80
    • 0034635221 scopus 로고    scopus 로고
    • Roles of PLC-beta2 and -beta3 and PI3Kgamma in chemoattractant-mediated signal transduction
    • Li Z., Jiang H., Xie W., Zhang Z., Smrcka A.V., and Wu D. Roles of PLC-beta2 and -beta3 and PI3Kgamma in chemoattractant-mediated signal transduction. Science 287 (2000) 1046-1049
    • (2000) Science , vol.287 , pp. 1046-1049
    • Li, Z.1    Jiang, H.2    Xie, W.3    Zhang, Z.4    Smrcka, A.V.5    Wu, D.6
  • 85
    • 23844462453 scopus 로고    scopus 로고
    • Cutting edge: T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase
    • Webb L.M., Vigorito E., Wymann M.P., Hirsch E., and Turner M. Cutting edge: T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase. J. Immunol. 175 (2005) 2783-2787
    • (2005) J. Immunol. , vol.175 , pp. 2783-2787
    • Webb, L.M.1    Vigorito, E.2    Wymann, M.P.3    Hirsch, E.4    Turner, M.5
  • 87
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase
    • Suzuki H., Terauchi Y., Fujiwara M., Aizawa S., Yazaki Y., Kadowaki T., and Koyasu S. Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase. Science 283 (1999) 390-392
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1    Terauchi, Y.2    Fujiwara, M.3    Aizawa, S.4    Yazaki, Y.5    Kadowaki, T.6    Koyasu, S.7
  • 88
    • 34247169493 scopus 로고    scopus 로고
    • p110delta is required for innate immunity to transplantable lymphomas
    • Saudemont A., Okkenhaug K., and Colucci F. p110delta is required for innate immunity to transplantable lymphomas. Biochem. Soc. Trans. 35 (2007) 183-185
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 183-185
    • Saudemont, A.1    Okkenhaug, K.2    Colucci, F.3
  • 89
    • 36148992966 scopus 로고    scopus 로고
    • The p110delta catalytic isoform of PI3K is a key player in NK cell development and cytokine secretion
    • Kim N., Saudemont A., Webb L., Camps M., Ruckle T., Hirsch E., Turner M., and Colucci F. The p110delta catalytic isoform of PI3K is a key player in NK cell development and cytokine secretion. Blood (2007)
    • (2007) Blood
    • Kim, N.1    Saudemont, A.2    Webb, L.3    Camps, M.4    Ruckle, T.5    Hirsch, E.6    Turner, M.7    Colucci, F.8
  • 95
    • 14644403593 scopus 로고    scopus 로고
    • NTAL/LAB and LAT: a balancing act in mast-cell activation and function
    • Rivera J. NTAL/LAB and LAT: a balancing act in mast-cell activation and function. Trends Immunol. 26 (2005) 119-122
    • (2005) Trends Immunol. , vol.26 , pp. 119-122
    • Rivera, J.1
  • 97
    • 34247572895 scopus 로고    scopus 로고
    • New developments in FcepsilonRI regulation, function and inhibition
    • Kraft S., and Kinet J.P. New developments in FcepsilonRI regulation, function and inhibition. Nat. Rev., Immunol. 7 (2007) 365-378
    • (2007) Nat. Rev., Immunol. , vol.7 , pp. 365-378
    • Kraft, S.1    Kinet, J.P.2
  • 99
    • 0038011833 scopus 로고    scopus 로고
    • Evolving concepts of rheumatoid arthritis
    • Firestein G.S. Evolving concepts of rheumatoid arthritis. Nature 423 (2003) 356-361
    • (2003) Nature , vol.423 , pp. 356-361
    • Firestein, G.S.1
  • 100
    • 34247098873 scopus 로고    scopus 로고
    • Auto-antibodies and autoreactive T-cells in rheumatoid arthritis: pathogenetic players and diagnostic tools
    • Steiner G. Auto-antibodies and autoreactive T-cells in rheumatoid arthritis: pathogenetic players and diagnostic tools. Clin. Rev. Allergy Immunol. 32 (2007) 23-36
    • (2007) Clin. Rev. Allergy Immunol. , vol.32 , pp. 23-36
    • Steiner, G.1
  • 103
    • 0020329644 scopus 로고
    • Collagen arthritis as a relevant model for rheumatoid arthritis
    • Trentham D.E. Collagen arthritis as a relevant model for rheumatoid arthritis. Arthritis Rheum. 25 (1982) 911-916
    • (1982) Arthritis Rheum. , vol.25 , pp. 911-916
    • Trentham, D.E.1
  • 107
    • 0025875259 scopus 로고
    • Lpr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease
    • Cohen P.L., and Eisenberg R.A. Lpr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease. Annu. Rev. Immunol. 9 (1991) 243-269
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 243-269
    • Cohen, P.L.1    Eisenberg, R.A.2
  • 111
    • 0035043299 scopus 로고    scopus 로고
    • Treatment of lupus with corticosteroids
    • Chatham W.W., and Kimberly R.P. Treatment of lupus with corticosteroids. Lupus 10 (2001) 140-147
    • (2001) Lupus , vol.10 , pp. 140-147
    • Chatham, W.W.1    Kimberly, R.P.2
  • 112
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis A.J. Atherosclerosis. Nature 407 (2000) 233-241
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 113
    • 0035936802 scopus 로고    scopus 로고
    • Atherosclerosis. The road ahead
    • Glass C.K., and Witztum J.L. Atherosclerosis. The road ahead. Cell 104 (2001) 503-516
    • (2001) Cell , vol.104 , pp. 503-516
    • Glass, C.K.1    Witztum, J.L.2
  • 114
    • 0034091794 scopus 로고    scopus 로고
    • Sites of action of protein kinase C and phosphatidylinositol 3-kinase are distinct in oxidized low density lipoprotein-induced macrophage proliferation
    • Biwa T., Sakai M., Matsumura T., Kobori S., Kaneko K., Miyazaki A., Hakamata H., Horiuchi S., and Shichiri M. Sites of action of protein kinase C and phosphatidylinositol 3-kinase are distinct in oxidized low density lipoprotein-induced macrophage proliferation. J. Biol. Chem. 275 (2000) 5810-5816
    • (2000) J. Biol. Chem. , vol.275 , pp. 5810-5816
    • Biwa, T.1    Sakai, M.2    Matsumura, T.3    Kobori, S.4    Kaneko, K.5    Miyazaki, A.6    Hakamata, H.7    Horiuchi, S.8    Shichiri, M.9
  • 115
    • 0034570598 scopus 로고    scopus 로고
    • Granulocyte/macrophage colony-stimulating factor plays an essential role in oxidized low density lipoprotein-induced macrophage proliferation
    • Biwa T., Sakai M., Shichiri M., and Horiuchi S. Granulocyte/macrophage colony-stimulating factor plays an essential role in oxidized low density lipoprotein-induced macrophage proliferation. J. Atheroscler. Thromb. 7 (2000) 14-20
    • (2000) J. Atheroscler. Thromb. , vol.7 , pp. 14-20
    • Biwa, T.1    Sakai, M.2    Shichiri, M.3    Horiuchi, S.4
  • 116
    • 0026725757 scopus 로고
    • Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells
    • Plump A.S., Smith J.D., Hayek T., Aalto-Setala K., Walsh A., Verstuyft J.G., Rubin E.M., and Breslow J.L. Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells. Cell 71 (1992) 343-353
    • (1992) Cell , vol.71 , pp. 343-353
    • Plump, A.S.1    Smith, J.D.2    Hayek, T.3    Aalto-Setala, K.4    Walsh, A.5    Verstuyft, J.G.6    Rubin, E.M.7    Breslow, J.L.8
  • 117
    • 0027958084 scopus 로고
    • ApoE-deficient mice develop lesions of all phases of atherosclerosis throughout the arterial tree
    • Nakashima Y., Plump A.S., Raines E.W., Breslow J.L., and Ross R. ApoE-deficient mice develop lesions of all phases of atherosclerosis throughout the arterial tree. Arterioscler. Thromb. 14 (1994) 133-140
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 133-140
    • Nakashima, Y.1    Plump, A.S.2    Raines, E.W.3    Breslow, J.L.4    Ross, R.5
  • 120
    • 33847279025 scopus 로고    scopus 로고
    • Pathogenesis and therapy of psoriasis
    • Lowes M.A., Bowcock A.M., and Krueger J.G. Pathogenesis and therapy of psoriasis. Nature 445 (2007) 866-873
    • (2007) Nature , vol.445 , pp. 866-873
    • Lowes, M.A.1    Bowcock, A.M.2    Krueger, J.G.3
  • 122
    • 18344364158 scopus 로고    scopus 로고
    • COPD unwound
    • Shapiro S.D. COPD unwound. N. Engl. J. Med. 352 (2005) 2016-2019
    • (2005) N. Engl. J. Med. , vol.352 , pp. 2016-2019
    • Shapiro, S.D.1
  • 123
    • 33947358942 scopus 로고    scopus 로고
    • Therapeutic potential of phosphatidylinositol 3-kinase inhibitors in inflammatory respiratory disease
    • Ito K., Caramori G., and Adcock I.M. Therapeutic potential of phosphatidylinositol 3-kinase inhibitors in inflammatory respiratory disease. J. Pharmacol. Exp. Ther. 321 (2007) 1-8
    • (2007) J. Pharmacol. Exp. Ther. , vol.321 , pp. 1-8
    • Ito, K.1    Caramori, G.2    Adcock, I.M.3
  • 124
    • 33749059726 scopus 로고    scopus 로고
    • The neurobiology of multiple sclerosis: genes, inflammation, and neurodegeneration
    • Hauser S.L., and Oksenberg J.R. The neurobiology of multiple sclerosis: genes, inflammation, and neurodegeneration. Neuron 52 (2006) 61-76
    • (2006) Neuron , vol.52 , pp. 61-76
    • Hauser, S.L.1    Oksenberg, J.R.2
  • 125
    • 0036546066 scopus 로고    scopus 로고
    • New concepts in the immunopathogenesis of multiple sclerosis
    • Hemmer B., Archelos J.J., and Hartung H.P. New concepts in the immunopathogenesis of multiple sclerosis. Nat. Rev., Neurosci. 3 (2002) 291-301
    • (2002) Nat. Rev., Neurosci. , vol.3 , pp. 291-301
    • Hemmer, B.1    Archelos, J.J.2    Hartung, H.P.3
  • 131
    • 34247178388 scopus 로고    scopus 로고
    • Isoform-selective PI3K inhibitors as novel therapeutics for the treatment of acute myocardial infarction
    • Doukas J., Wrasidlo W., Noronha G., Dneprovskaia E., Hood J., and Soll R. Isoform-selective PI3K inhibitors as novel therapeutics for the treatment of acute myocardial infarction. Biochem. Soc. Trans. 35 (2007) 204-206
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 204-206
    • Doukas, J.1    Wrasidlo, W.2    Noronha, G.3    Dneprovskaia, E.4    Hood, J.5    Soll, R.6
  • 133
    • 28844448182 scopus 로고    scopus 로고
    • Oncogenic PI3K deregulates transcription and translation
    • Bader A.G., Kang S., Zhao L., and Vogt P.K. Oncogenic PI3K deregulates transcription and translation. Nat. Rev., Cancer 5 (2005) 921-929
    • (2005) Nat. Rev., Cancer , vol.5 , pp. 921-929
    • Bader, A.G.1    Kang, S.2    Zhao, L.3    Vogt, P.K.4
  • 134
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI(3)K and mTOR signalling controls tumour cell growth
    • Shaw R.J., and Cantley L.C. Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441 (2006) 424-430
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 135
    • 0036206130 scopus 로고    scopus 로고
    • Protean PTEN: form and function
    • Waite K.A., and Eng C. Protean PTEN: form and function. Am. J. Hum. Genet. 70 (2002) 829-844
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 829-844
    • Waite, K.A.1    Eng, C.2
  • 136
    • 0042316755 scopus 로고    scopus 로고
    • PTEN: one gene, many syndromes
    • Eng C. PTEN: one gene, many syndromes. Human Mutat. 22 (2003) 183-198
    • (2003) Human Mutat. , vol.22 , pp. 183-198
    • Eng, C.1
  • 140
    • 0034701247 scopus 로고    scopus 로고
    • Germline and germline mosaic PTEN mutations associated with a Proteus-like syndrome of hemihypertrophy, lower limb asymmetry, arteriovenous malformations and lipomatosis
    • Zhou X.P., Marsh D.J., Hampel H., Mulliken J.B., Gimm O., and Eng C. Germline and germline mosaic PTEN mutations associated with a Proteus-like syndrome of hemihypertrophy, lower limb asymmetry, arteriovenous malformations and lipomatosis. Hum. Mol. Genet. 9 (2000) 765-768
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 765-768
    • Zhou, X.P.1    Marsh, D.J.2    Hampel, H.3    Mulliken, J.B.4    Gimm, O.5    Eng, C.6
  • 141
    • 0033738748 scopus 로고    scopus 로고
    • Will the real Cowden syndrome please stand up: revised diagnostic criteria
    • Eng C. Will the real Cowden syndrome please stand up: revised diagnostic criteria. J. Med. Genet. 37 (2000) 828-830
    • (2000) J. Med. Genet. , vol.37 , pp. 828-830
    • Eng, C.1
  • 144
    • 0038456399 scopus 로고    scopus 로고
    • PTEN signaling pathways in melanoma
    • Wu H., Goel V., and Haluska F.G. PTEN signaling pathways in melanoma. Oncogene 22 (2003) 3113-3122
    • (2003) Oncogene , vol.22 , pp. 3113-3122
    • Wu, H.1    Goel, V.2    Haluska, F.G.3
  • 150
    • 0037057508 scopus 로고    scopus 로고
    • Genetic alterations in cervical carcinomas: frequent low-level amplifications of oncogenes are associated with human papillomavirus infection
    • Zhang A., Maner S., Betz R., Angstrom T., Stendahl U., Bergman F., Zetterberg A., and Wallin K.L. Genetic alterations in cervical carcinomas: frequent low-level amplifications of oncogenes are associated with human papillomavirus infection. Int. J. Cancer 101 (2002) 427-433
    • (2002) Int. J. Cancer , vol.101 , pp. 427-433
    • Zhang, A.1    Maner, S.2    Betz, R.3    Angstrom, T.4    Stendahl, U.5    Bergman, F.6    Zetterberg, A.7    Wallin, K.L.8
  • 151
    • 0033119702 scopus 로고    scopus 로고
    • Expression analysis of genes at 3q26-q27 involved in frequent amplification in squamous cell lung carcinoma
    • Racz A., Brass N., Heckel D., Pahl S., Remberger K., and Meese E. Expression analysis of genes at 3q26-q27 involved in frequent amplification in squamous cell lung carcinoma. Eur. J. Cancer 35 (1999) 641-646
    • (1999) Eur. J. Cancer , vol.35 , pp. 641-646
    • Racz, A.1    Brass, N.2    Heckel, D.3    Pahl, S.4    Remberger, K.5    Meese, E.6
  • 152
    • 33646706052 scopus 로고    scopus 로고
    • Oncogenic PI3K and its role in cancer
    • Samuels Y., and Ericson K. Oncogenic PI3K and its role in cancer. Curr. Opin. Oncol. 18 (2006) 77-82
    • (2006) Curr. Opin. Oncol. , vol.18 , pp. 77-82
    • Samuels, Y.1    Ericson, K.2
  • 156
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang S., Bader A.G., and Vogt P.K. Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 802-807
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 802-807
    • Kang, S.1    Bader, A.G.2    Vogt, P.K.3
  • 160
    • 0037524354 scopus 로고    scopus 로고
    • LKB1, a protein kinase regulating cell proliferation and polarity
    • Boudeau J., Sapkota G., and Alessi D.R. LKB1, a protein kinase regulating cell proliferation and polarity. FEBS Lett. 546 (2003) 159-165
    • (2003) FEBS Lett. , vol.546 , pp. 159-165
    • Boudeau, J.1    Sapkota, G.2    Alessi, D.R.3
  • 161
    • 2342559981 scopus 로고    scopus 로고
    • The TOR pathway: a target for cancer therapy
    • Bjornsti M.A., and Houghton P.J. The TOR pathway: a target for cancer therapy. Nat. Rev., Cancer 4 (2004) 335-348
    • (2004) Nat. Rev., Cancer , vol.4 , pp. 335-348
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 162
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin D.A., and Sabatini D.M. Defining the role of mTOR in cancer. Cancer Cell 12 (2007) 9-22
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 164
  • 165
    • 34249679614 scopus 로고    scopus 로고
    • mTOR Complex1-S6K1 signaling: at the crossroads of obesity, diabetes and cancer
    • Dann S.G., Selvaraj A., and Thomas G. mTOR Complex1-S6K1 signaling: at the crossroads of obesity, diabetes and cancer. Trends Mol. Med. 13 (2007) 252-259
    • (2007) Trends Mol. Med. , vol.13 , pp. 252-259
    • Dann, S.G.1    Selvaraj, A.2    Thomas, G.3
  • 170
    • 33750684953 scopus 로고    scopus 로고
    • Role of insulin, adipocyte hormones, and nutrient-sensing pathways in regulating fuel metabolism and energy homeostasis: a nutritional perspective of diabetes, obesity, and cancer
    • Marshall S. Role of insulin, adipocyte hormones, and nutrient-sensing pathways in regulating fuel metabolism and energy homeostasis: a nutritional perspective of diabetes, obesity, and cancer. Sci. STKE 2006 (2006) re7
    • (2006) Sci. STKE , vol.2006
    • Marshall, S.1
  • 174
    • 23644448924 scopus 로고    scopus 로고
    • Increased p85/55/50 expression and decreased phosphotidylinositol 3-kinase activity in insulin-resistant human skeletal muscle
    • Bandyopadhyay G.K., Yu J.G., Ofrecio J., and Olefsky J.M. Increased p85/55/50 expression and decreased phosphotidylinositol 3-kinase activity in insulin-resistant human skeletal muscle. Diabetes 54 (2005) 2351-2359
    • (2005) Diabetes , vol.54 , pp. 2351-2359
    • Bandyopadhyay, G.K.1    Yu, J.G.2    Ofrecio, J.3    Olefsky, J.M.4
  • 176
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann M.P., Bulgarelli-Leva G., Zvelebil M.J., Pirola L., Vanhaesebroeck B., Waterfield M.D., and Panayotou G. Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 16 (1996) 1722-1733
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarelli-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 177
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro A., and Wymann M.P. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 296 (1993) 297-301
    • (1993) Biochem. J. , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 178
    • 0027374488 scopus 로고
    • Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells
    • Yano H., Nakanishi S., Kimura K., Hanai N., Saitoh Y., Fukui Y., Nonomura Y., and Matsuda Y. Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J. Biol. Chem. 268 (1993) 25846-25856
    • (1993) J. Biol. Chem. , vol.268 , pp. 25846-25856
    • Yano, H.1    Nakanishi, S.2    Kimura, K.3    Hanai, N.4    Saitoh, Y.5    Fukui, Y.6    Nonomura, Y.7    Matsuda, Y.8
  • 179
    • 0028326907 scopus 로고
    • Platelet-derived growth factor-induced phosphatidylinositol 3-kinase activation mediates actin rearrangements in fibroblasts
    • (298 Pt.)
    • Wymann M., and Arcaro A. Platelet-derived growth factor-induced phosphatidylinositol 3-kinase activation mediates actin rearrangements in fibroblasts. Biochem. J. 3 (1994) 517-520 (298 Pt.)
    • (1994) Biochem. J. , vol.3 , pp. 517-520
    • Wymann, M.1    Arcaro, A.2
  • 180
    • 0028170210 scopus 로고
    • 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., and Brown R.F. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269 (1994) 5241-5248
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 182
    • 4944239923 scopus 로고    scopus 로고
    • Design strategies for protein kinase inhibitors
    • Parang K., and Sun G. Design strategies for protein kinase inhibitors. Curr. Opin. Drug Discov. Dev. 7 (2004) 617-629
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 617-629
    • Parang, K.1    Sun, G.2
  • 183
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights into phosphoinositide 3-kinase catalysis and signalling
    • Walker E.H., Perisic O., Ried C., Stephens L., and Williams R.L. Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature 402 (1999) 313-320
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 184
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T., Wymann M.P., and Williams R.L. Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6 (2000) 909-919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 185
    • 0030920653 scopus 로고    scopus 로고
    • Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: structure-activity analysis and interactions with wortmannin
    • Stoyanova S., Bulgarelli-Leva G., Kirsch C., Hanck T., Klinger R., Wetzker R., and Wymann M.P. Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: structure-activity analysis and interactions with wortmannin. Biochem. J. 324 (1997) 489-495
    • (1997) Biochem. J. , vol.324 , pp. 489-495
    • Stoyanova, S.1    Bulgarelli-Leva, G.2    Kirsch, C.3    Hanck, T.4    Klinger, R.5    Wetzker, R.6    Wymann, M.P.7
  • 188
    • 37049136393 scopus 로고
    • Fungal products: Part III. Structure of wortmannin and some hydrolysis products
    • MacMillan J., Vanstone A.E., and Yeboah S.K. Fungal products: Part III. Structure of wortmannin and some hydrolysis products. J. Chem. Soc. 1 (1972) 2898-2903
    • (1972) J. Chem. Soc. , vol.1 , pp. 2898-2903
    • MacMillan, J.1    Vanstone, A.E.2    Yeboah, S.K.3
  • 189
    • 0343561751 scopus 로고
    • Fungal products: Part 21. Biosynthesis of the fungal metabolite, wortmannin, from (1,2-13C2)-acetate
    • Simpson T.J., Lunnon M.W., and MacMillan J. Fungal products: Part 21. Biosynthesis of the fungal metabolite, wortmannin, from (1,2-13C2)-acetate. J. Chem. Soc., Perkin Trans. 1 (1979) 931-934
    • (1979) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 931-934
    • Simpson, T.J.1    Lunnon, M.W.2    MacMillan, J.3
  • 190
    • 37049126596 scopus 로고
    • Crystal structure and absolute configuration of wortmannin and of wortmannin p-bromobenzoate
    • Petcher T.J., Weber H., and Kis Z. Crystal structure and absolute configuration of wortmannin and of wortmannin p-bromobenzoate. J. Chem. Soc., Chem. Commun. (1972) 1061-1062
    • (1972) J. Chem. Soc., Chem. Commun. , pp. 1061-1062
    • Petcher, T.J.1    Weber, H.2    Kis, Z.3
  • 191
    • 0023150655 scopus 로고
    • Inhibition of the phagocytosis-induced respiratory burst by the fungal metabolite wortmannin and some analogues
    • Baggiolini M., Dewald B., Schnyder J., Ruch W., Cooper P.H., and Payne T.G. Inhibition of the phagocytosis-induced respiratory burst by the fungal metabolite wortmannin and some analogues. Exp. Cell Res. 169 (1987) 408-418
    • (1987) Exp. Cell Res. , vol.169 , pp. 408-418
    • Baggiolini, M.1    Dewald, B.2    Schnyder, J.3    Ruch, W.4    Cooper, P.H.5    Payne, T.G.6
  • 192
    • 0028321727 scopus 로고
    • Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes
    • Thelen M., Wymann M.P., and Langen H. Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 4960-4964
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4960-4964
    • Thelen, M.1    Wymann, M.P.2    Langen, H.3
  • 193
    • 20844458056 scopus 로고    scopus 로고
    • Chemistry and biology of wortmannin
    • Wipf P., and Halter R.J. Chemistry and biology of wortmannin. Org. Biomol. Chem. 3 (2005) 2053-2061
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 2053-2061
    • Wipf, P.1    Halter, R.J.2
  • 195
    • 0028197377 scopus 로고
    • A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase
    • Woscholski R., Kodaki T., McKinnon M., Waterfield M.D., and Parker P.J. A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase. FEBS Lett. 342 (1994) 109-114
    • (1994) FEBS Lett. , vol.342 , pp. 109-114
    • Woscholski, R.1    Kodaki, T.2    McKinnon, M.3    Waterfield, M.D.4    Parker, P.J.5
  • 199
    • 0029831167 scopus 로고    scopus 로고
    • 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., Sabers C., Wiederrecht G., Lawrence J.C.J., and Abraham R.T. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15 (1996) 5256-5267
    • (1996) EMBO J. , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence, J.C.J.5    Abraham, R.T.6
  • 200
    • 0032189483 scopus 로고    scopus 로고
    • Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin
    • Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E., and Abraham R.T. Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin. Cancer Res. 58 (1998) 4375-4382
    • (1998) Cancer Res. , vol.58 , pp. 4375-4382
    • Sarkaria, J.N.1    Tibbetts, R.S.2    Busby, E.C.3    Kennedy, A.P.4    Hill, D.E.5    Abraham, R.T.6
  • 204
    • 33645001286 scopus 로고    scopus 로고
    • Synthesis of fluorescent derivatives of wortmannin and demethoxyviridin as probes for phosphatidylinositol 3-kinase
    • Giner J.L., Kehbein K.A., Cook J.A., Smith M.C., Vlahos C.J., and Badwey J.A. Synthesis of fluorescent derivatives of wortmannin and demethoxyviridin as probes for phosphatidylinositol 3-kinase. Bioorg. Med. Chem. Lett. 16 (2006) 2518-2521
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 2518-2521
    • Giner, J.L.1    Kehbein, K.A.2    Cook, J.A.3    Smith, M.C.4    Vlahos, C.J.5    Badwey, J.A.6
  • 207
    • 12344256951 scopus 로고    scopus 로고
    • Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase
    • Liu Y., Shreder K.R., Gai W., Corral S., Ferris D.K., and Rosenblum J.S. Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase. Chem. Biol. 12 (2005) 99-107
    • (2005) Chem. Biol. , vol.12 , pp. 99-107
    • Liu, Y.1    Shreder, K.R.2    Gai, W.3    Corral, S.4    Ferris, D.K.5    Rosenblum, J.S.6
  • 208
    • 34047276295 scopus 로고    scopus 로고
    • Polo-like kinases inhibited by wortmannin. Labeling site and downstream effects
    • Liu Y., Jiang N., Wu J., Dai W., and Rosenblum J.S. Polo-like kinases inhibited by wortmannin. Labeling site and downstream effects. J. Biol. Chem. 282 (2007) 2505-2511
    • (2007) J. Biol. Chem. , vol.282 , pp. 2505-2511
    • Liu, Y.1    Jiang, N.2    Wu, J.3    Dai, W.4    Rosenblum, J.S.5
  • 210
    • 0037020224 scopus 로고    scopus 로고
    • Direct effects of caffeine and theophylline on p110 delta and other phosphoinositide 3-kinases. Differential effects on lipid kinase and protein kinase activities
    • Foukas L.C., Daniele N., Ktori C., Anderson K.E., Jensen J., and Shepherd P.R. Direct effects of caffeine and theophylline on p110 delta and other phosphoinositide 3-kinases. Differential effects on lipid kinase and protein kinase activities. J. Biol. Chem. 277 (2002) 37124-37130
    • (2002) J. Biol. Chem. , vol.277 , pp. 37124-37130
    • Foukas, L.C.1    Daniele, N.2    Ktori, C.3    Anderson, K.E.4    Jensen, J.5    Shepherd, P.R.6
  • 211
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur J.A., and Sinclair D.A. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev., Drug Discov. 5 (2006) 493-506
    • (2006) Nat. Rev., Drug Discov. , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 212
    • 0002256765 scopus 로고
    • Concentration of the phytoalexin resveratrol in wine
    • Siemann E.H., and Creasy L.L. Concentration of the phytoalexin resveratrol in wine. Am. J. Enol. Vitic. 43 (1992) 49-52
    • (1992) Am. J. Enol. Vitic. , vol.43 , pp. 49-52
    • Siemann, E.H.1    Creasy, L.L.2
  • 213
    • 34548730196 scopus 로고    scopus 로고
    • Resveratrol is a class IA phosphoinositide 3-kinase inhibitor
    • Frojdo S., Cozzone D., Vidal H., and Pirola L. Resveratrol is a class IA phosphoinositide 3-kinase inhibitor. Biochem. J. 406 (2007) 511-518
    • (2007) Biochem. J. , vol.406 , pp. 511-518
    • Frojdo, S.1    Cozzone, D.2    Vidal, H.3    Pirola, L.4
  • 217
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement
    • Sadhu C., Masinovsky B., Dick K., Sowell C.G., and Staunton D.E. Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement. J. Immunol. 170 (2003) 2647-2654
    • (2003) J. Immunol. , vol.170 , pp. 2647-2654
    • Sadhu, C.1    Masinovsky, B.2    Dick, K.3    Sowell, C.G.4    Staunton, D.E.5
  • 220
    • 33750459743 scopus 로고    scopus 로고
    • A selective inhibitor of the p110delta isoform of PI 3-kinase inhibits AML cell proliferation and survival and increases the cytotoxic effects of VP16
    • Billottet C., Grandage V.L., Gale R.E., Quattropani A., Rommel C., Vanhaesebroeck B., and Khwaja A. A selective inhibitor of the p110delta isoform of PI 3-kinase inhibits AML cell proliferation and survival and increases the cytotoxic effects of VP16. Oncogene 25 (2006) 6648-6659
    • (2006) Oncogene , vol.25 , pp. 6648-6659
    • Billottet, C.1    Grandage, V.L.2    Gale, R.E.3    Quattropani, A.4    Rommel, C.5    Vanhaesebroeck, B.6    Khwaja, A.7
  • 231
    • 34548473308 scopus 로고    scopus 로고
    • Discovery of 3,3′-(2,4-diaminopteridine-6,7-diyl)diphenol as an isozyme-selective inhibitor of PI3K for the treatment of ischemia reperfusion injury associated with myocardial infarction
    • Palanki M.S., Dneprovskaia E., Doukas J., Fine R.M., Hood J., Kang X., Lohse D., Martin M., Noronha G., Soll R.M., Wrasidlo W., Yee S., and Zhu H. Discovery of 3,3′-(2,4-diaminopteridine-6,7-diyl)diphenol as an isozyme-selective inhibitor of PI3K for the treatment of ischemia reperfusion injury associated with myocardial infarction. J. Med. Chem. 50 (2007) 4279-4294
    • (2007) J. Med. Chem. , vol.50 , pp. 4279-4294
    • Palanki, M.S.1    Dneprovskaia, E.2    Doukas, J.3    Fine, R.M.4    Hood, J.5    Kang, X.6    Lohse, D.7    Martin, M.8    Noronha, G.9    Soll, R.M.10    Wrasidlo, W.11    Yee, S.12    Zhu, H.13
  • 232
    • 34247211775 scopus 로고    scopus 로고
    • Identification of a small-molecule inhibitor of class Ia PI3Ks with cell-based screening
    • Yang J., Shamji A., Matchacheep S., and Schreiber S.L. Identification of a small-molecule inhibitor of class Ia PI3Ks with cell-based screening. Chem. Biol. 14 (2007) 371-377
    • (2007) Chem. Biol. , vol.14 , pp. 371-377
    • Yang, J.1    Shamji, A.2    Matchacheep, S.3    Schreiber, S.L.4
  • 233
    • 0028601306 scopus 로고
    • Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene
    • Volinia S., Hiles I., Ormondroyd E., Nizetic D., Antonacci R., Rocchi M., and Waterfield M.D. Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene. Genomics 24 (1994) 472-477
    • (1994) Genomics , vol.24 , pp. 472-477
    • Volinia, S.1    Hiles, I.2    Ormondroyd, E.3    Nizetic, D.4    Antonacci, R.5    Rocchi, M.6    Waterfield, M.D.7
  • 234
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu P., Mondino A., Skolnik E.Y., and Schlessinger J. Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol. Cell. Biol. 13 (1993) 7677-7688
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7677-7688
    • Hu, P.1    Mondino, A.2    Skolnik, E.Y.3    Schlessinger, J.4
  • 236
    • 0031592814 scopus 로고    scopus 로고
    • Identification and chromosome assignment of a human gene encoding a novel phosphatidylinositol-3 kinase
    • Seki N., Nimura Y., Ohira M., Saito T., Ichimiya S., Nomura N., and Nakagawara A. Identification and chromosome assignment of a human gene encoding a novel phosphatidylinositol-3 kinase. DNA Res. 4 (1997) 355-358
    • (1997) DNA Res. , vol.4 , pp. 355-358
    • Seki, N.1    Nimura, Y.2    Ohira, M.3    Saito, T.4    Ichimiya, S.5    Nomura, N.6    Nakagawara, A.7
  • 239
    • 7144257177 scopus 로고    scopus 로고
    • An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta subunit and HUMORF8, a putative deubiquitinating enzyme
    • Janssen J.W., Schleithoff L., Bartram C.R., and Schulz A.S. An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta subunit and HUMORF8, a putative deubiquitinating enzyme. Oncogene 16 (1998) 1767-1772
    • (1998) Oncogene , vol.16 , pp. 1767-1772
    • Janssen, J.W.1    Schleithoff, L.2    Bartram, C.R.3    Schulz, A.S.4
  • 240
    • 0032536905 scopus 로고    scopus 로고
    • Cloning of human p55 gamma, a regulatory subunit of phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen with the insulin-like growth factor-I receptor
    • Dey B.R., Furlanetto R.W., and Nissley S.P. Cloning of human p55 gamma, a regulatory subunit of phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen with the insulin-like growth factor-I receptor. Gene 209 (1998) 175-183
    • (1998) Gene , vol.209 , pp. 175-183
    • Dey, B.R.1    Furlanetto, R.W.2    Nissley, S.P.3
  • 242
    • 15744363780 scopus 로고    scopus 로고
    • p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma
    • Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P., and Stephens L. p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma. Curr. Biol. 15 (2005) 566-570
    • (2005) Curr. Biol. , vol.15 , pp. 566-570
    • Suire, S.1    Coadwell, J.2    Ferguson, G.J.3    Davidson, K.4    Hawkins, P.5    Stephens, L.6
  • 243
    • 0030884527 scopus 로고    scopus 로고
    • Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
    • Domin J., Pages F., Volinia S., Rittenhouse S.E., Zvelebil M.J., Stein R.C., and Waterfield M.D. Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin. Biochem. J. 326 (1997) 139-147
    • (1997) Biochem. J. , vol.326 , pp. 139-147
    • Domin, J.1    Pages, F.2    Volinia, S.3    Rittenhouse, S.E.4    Zvelebil, M.J.5    Stein, R.C.6    Waterfield, M.D.7
  • 244
    • 0031575938 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K
    • Brown R.A., Ho L.K., Weber-Hall S.J., Shipley J.M., and Fry M.J. Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K. Biochem. Biophys. Res. Commun. 233 (1997) 537-544
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 537-544
    • Brown, R.A.1    Ho, L.K.2    Weber-Hall, S.J.3    Shipley, J.M.4    Fry, M.J.5
  • 245
    • 0032534892 scopus 로고    scopus 로고
    • cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12
    • Rozycka M., Lu Y.J., Brown R.A., Lau M.R., Shipley J.M., and Fry M.J. cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12. Genomics 54 (1998) 569-574
    • (1998) Genomics , vol.54 , pp. 569-574
    • Rozycka, M.1    Lu, Y.J.2    Brown, R.A.3    Lau, M.R.4    Shipley, J.M.5    Fry, M.J.6
  • 247
    • 0031026639 scopus 로고    scopus 로고
    • Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex
    • Panaretou C., Domin J., Cockcroft S., and Waterfield M.D. Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex. J. Biol. Chem. 272 (1997) 2477-2485
    • (1997) J. Biol. Chem. , vol.272 , pp. 2477-2485
    • Panaretou, C.1    Domin, J.2    Cockcroft, S.3    Waterfield, M.D.4
  • 248
    • 0028032480 scopus 로고
    • Cloning and characterization of a human phosphatidylinositol 4-kinase
    • Wong K., and Cantley L.C. Cloning and characterization of a human phosphatidylinositol 4-kinase. J. Biol. Chem. 269 (1994) 28878-28884
    • (1994) J. Biol. Chem. , vol.269 , pp. 28878-28884
    • Wong, K.1    Cantley, L.C.2
  • 249
    • 0031054245 scopus 로고    scopus 로고
    • Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase
    • Meyers R., and Cantley L.C. Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase. J. Biol. Chem. 272 (1997) 4384-4390
    • (1997) J. Biol. Chem. , vol.272 , pp. 4384-4390
    • Meyers, R.1    Cantley, L.C.2
  • 251
    • 0029111784 scopus 로고
    • Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8
    • Sipley J.D., Menninger J.C., Hartley K.O., Ward D.C., Jackson S.P., and Anderson C.W. Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 7515-7519
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7515-7519
    • Sipley, J.D.1    Menninger, J.C.2    Hartley, K.O.3    Ward, D.C.4    Jackson, S.P.5    Anderson, C.W.6
  • 254
    • 0029655983 scopus 로고    scopus 로고
    • Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo
    • Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., and Moscat J. Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. Mol. Cell. Biol. 16 (1996) 105-114
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 105-114
    • Diaz-Meco, M.T.1    Municio, M.M.2    Sanchez, P.3    Lozano, J.4    Moscat, J.5
  • 255
    • 0035449691 scopus 로고    scopus 로고
    • Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay
    • Yamashita A., Ohnishi T., Kashima I., Taya Y., and Ohno S. Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay. Genes Dev. 15 (2001) 2215-2228
    • (2001) Genes Dev. , vol.15 , pp. 2215-2228
    • Yamashita, A.1    Ohnishi, T.2    Kashima, I.3    Taya, Y.4    Ohno, S.5
  • 256
    • 0032493894 scopus 로고    scopus 로고
    • The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins
    • McMahon S.B., Van Buskirk H.A., Dugan K.A., Copeland T.D., and Cole M.D. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell 94 (1998) 363-374
    • (1998) Cell , vol.94 , pp. 363-374
    • McMahon, S.B.1    Van Buskirk, H.A.2    Dugan, K.A.3    Copeland, T.D.4    Cole, M.D.5
  • 261
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith G.C., and Jackson S.P. The DNA-dependent protein kinase. Genes Dev. 13 (1999) 916-934
    • (1999) Genes Dev. , vol.13 , pp. 916-934
    • Smith, G.C.1    Jackson, S.P.2
  • 266
    • 0037205494 scopus 로고    scopus 로고
    • Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments
    • Balla A., Tuymetova G., Barshishat M., Geiszt M., and Balla T. Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments. J. Biol. Chem. 277 (2002) 20041-20050
    • (2002) J. Biol. Chem. , vol.277 , pp. 20041-20050
    • Balla, A.1    Tuymetova, G.2    Barshishat, M.3    Geiszt, M.4    Balla, T.5


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