메뉴 건너뛰기




Volumn 18, Issue 5, 1999, Pages 1292-1302

Autophosphorylation of p110δ phosphoinositide 3-kinase: A new paradigm for the regulation of lipid kinases in vitro and in vivo

Author keywords

Autophosphorylation; Lipid; Phosphoinositide 3 kinase; Phosphospecific antibodies

Indexed keywords

ANTISERUM; CD28 ANTIGEN; OKADAIC ACID; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE; PROTEIN TYROSINE KINASE; SERINE; WORTMANNIN; 2 MORPHOLINO 8 PHENYLCHROMONE; 2-(4-MORPHOLINYL)-8-PHENYL-4H-1-BENZOPYRAN-4-ONE; ANDROSTANE DERIVATIVE; CHROMONE DERIVATIVE; MORPHOLINE DERIVATIVE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOPEPTIDE; PHOSPHOSERINE; RECOMBINANT PROTEIN;

EID: 0033104502     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (98)

References (57)
  • 1
    • 0029913340 scopus 로고    scopus 로고
    • Insulin receptor substrate 1 hinds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain
    • Antonetti, D.A., Algcnstaedt, P. and Kahn, C.R. (1996) Insulin receptor substrate 1 hinds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain. Mol. Cell. Biol., 16, 2195-2203.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2195-2203
    • Antonetti, D.A.1    Algcnstaedt, P.2    Kahn, C.R.3
  • 2
    • 0026660653 scopus 로고
    • Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation
    • Backer, J.M. et al. (1992) Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J., 11, 3469-3479.
    • (1992) EMBO J. , vol.11 , pp. 3469-3479
    • Backer, J.M.1
  • 3
    • 0032508504 scopus 로고    scopus 로고
    • Enhanced phosphorylation of p53 by ATM in response to DNA damage
    • Banin, S. et al. (1998) Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science, 281, 1674-1677.
    • (1998) Science , vol.281 , pp. 1674-1677
    • Banin, S.1
  • 4
    • 0032500730 scopus 로고    scopus 로고
    • Bifurcation of lipid and protein kinase signals of PI3Kγ to the protein kinases PKB and MAPK
    • Bondeva, T., Pirola, L., Bulgarelli-Leva, G., Rubio, I., Wetzker, R. and Wymann, M.P. (1998) Bifurcation of lipid and protein kinase signals of PI3Kγ to the protein kinases PKB and MAPK. Science, 282, 293-296.
    • (1998) Science , vol.282 , pp. 293-296
    • Bondeva, T.1    Pirola, L.2    Bulgarelli-Leva, G.3    Rubio, I.4    Wetzker, R.5    Wymann, M.P.6
  • 5
    • 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.,Jr and Abraham, R.T. (1996) Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J., 15, 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., Jr.5    Abraham, R.T.6
  • 9
  • 10
    • 0025291157 scopus 로고
    • Characterization of pp85, a target of oncogenes and growth factor receptors
    • Cohen, B., Liu, Y.X., Druker, B., Roberts, T.M. and Schaffhausen, B.S. (1990) Characterization of pp85, a target of oncogenes and growth factor receptors. Mol. Cell. Biol., 10, 2909-2915.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2909-2915
    • Cohen, B.1    Liu, Y.X.2    Druker, B.3    Roberts, T.M.4    Schaffhausen, B.S.5
  • 11
    • 0028157767 scopus 로고
    • PI 3-kinase: Structural and functional analysis of intersubunit interactions
    • Dhand, R. et al. (1994a) PI 3-kinase: structural and functional analysis of intersubunit interactions. EMBO J., 13, 511-521.
    • (1994) EMBO J. , vol.13 , pp. 511-521
    • Dhand, R.1
  • 12
    • 0027953284 scopus 로고
    • PI 3-kinase is a dual specificity enzyme: Autoregulation by an intrinsic protein-serine kinase activity
    • Dhand, R. et al. (1994b) PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity. EMBO J., 13, 522-533.
    • (1994) EMBO J. , vol.13 , pp. 522-533
    • Dhand, R.1
  • 13
    • 0029788889 scopus 로고    scopus 로고
    • Binding to the platelet-derived growth factor receptor transiently activates the p85α-p110α phosphoinositide 3-kinase complex in vivo
    • Domin, J., Dhand, R. and Waterfield, M.D. (1996) Binding to the platelet-derived growth factor receptor transiently activates the p85α-p110α phosphoinositide 3-kinase complex in vivo. J. Biol. Chem., 271, 21614-21621.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21614-21621
    • Domin, J.1    Dhand, R.2    Waterfield, M.D.3
  • 14
    • 0027232756 scopus 로고
    • A biosensor approach to probe the structure and function of the p85 α subunit of the phosphatidylinositol 3-kinase complex
    • End, P., Gout, I., Fry, M.J., Panayolou, G., Dhand, R., Yonezawa, K., Kasuga, M. and Waterfield, M.D. (1993) A biosensor approach to probe the structure and function of the p85 α subunit of the phosphatidylinositol 3-kinase complex. J. Biol. Chem., 268, 10066-10075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10066-10075
    • End, P.1    Gout, I.2    Fry, M.J.3    Panayolou, G.4    Dhand, R.5    Yonezawa, K.6    Kasuga, M.7    Waterfield, M.D.8
  • 15
    • 0032474612 scopus 로고    scopus 로고
    • Signal transduction. What goes up must come down
    • Evans, D.R. and Hemmings, B.A. (1998) Signal transduction. What goes up must come down. Nature, 394, 23-24.
    • (1998) Nature , vol.394 , pp. 23-24
    • Evans, D.R.1    Hemmings, B.A.2
  • 16
    • 0030907987 scopus 로고    scopus 로고
    • P13K: Downstream AKTion blocks apoptosis
    • Franke, T.F., Kaplan, D.R. and Cantley, L.C. (1997) P13K: downstream AKTion blocks apoptosis. Cell, 88, 435-437.
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 18
    • 0031060542 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines
    • He, Z., He, Y.S., Kim, Y., Chu, L., Ohmstede, C., Biron, K.K. and Coen, D.M. (1997) The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines. J. Virol., 71, 405-411.
    • (1997) J. Virol. , vol.71 , pp. 405-411
    • He, Z.1    He, Y.S.2    Kim, Y.3    Chu, L.4    Ohmstede, C.5    Biron, K.K.6    Coen, D.M.7
  • 19
    • 0028120902 scopus 로고
    • Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits
    • Holt, K.H., Olson, L., Moye-Rowley, W.S. and Pessin, J.E. (1994) Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits. Mol. Cell. Biol., 14, 42-49.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 42-49
    • Holt, K.H.1    Olson, L.2    Moye-Rowley, W.S.3    Pessin, J.E.4
  • 20
    • 0028918408 scopus 로고
    • Rasdependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu, Q., Klippel, A., Muslin, A.J., Fantl, W.J. and Williams, L.T. (1995) Rasdependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science, 268, 100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 21
    • 0028856331 scopus 로고
    • When is a lipid kinase not a lipid kinase? When it is a protein kinase
    • Hunter, T. (1995) When is a lipid kinase not a lipid kinase? When it is a protein kinase. Cell, 83, 1-4.
    • (1995) Cell , vol.83 , pp. 1-4
    • Hunter, T.1
  • 22
    • 0029895645 scopus 로고    scopus 로고
    • Purification and characterisation of human ZAP-70 protein-tyrosine kinase from a baculovirus expression system
    • Isakov, N., Wange, R.L., Watts, J.D., Aebersold, R. and Samelson, L.E. (1996) Purification and characterisation of human ZAP-70 protein-tyrosine kinase from a baculovirus expression system. J. Biol. Chem., 271, 15753-15761.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15753-15761
    • Isakov, N.1    Wange, R.L.2    Watts, J.D.3    Aebersold, R.4    Samelson, L.E.5
  • 23
    • 0032472913 scopus 로고    scopus 로고
    • Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3-kinase
    • Jimenez, C. et al. (1998) Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3-kinase. EMBO J., 17, 743-753.
    • (1998) EMBO J. , vol.17 , pp. 743-753
    • Jimenez, C.1
  • 24
    • 0023665111 scopus 로고
    • Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
    • Kaplan, D.R., Whitman, M., Schaffhausen, B., Pallas, D.C., White, M., Cantley, L. and Roberts, T.M. (1987) Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell, 50, 1021-1029.
    • (1987) Cell , vol.50 , pp. 1021-1029
    • Kaplan, D.R.1    Whitman, M.2    Schaffhausen, B.3    Pallas, D.C.4    White, M.5    Cantley, L.6    Roberts, T.M.7
  • 25
    • 0028800996 scopus 로고
    • PIK-related kinases: DNA repair, recombination and cell cycle checkpoints
    • Keith, C.T. and Schreiber, S.L. (1995) PIK-related kinases: DNA repair, recombination and cell cycle checkpoints. Science, 270, 50-51.
    • (1995) Science , vol.270 , pp. 50-51
    • Keith, C.T.1    Schreiber, S.L.2
  • 26
    • 0028198330 scopus 로고
    • The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity
    • Klippel, A., Escobedo, J.A., Hirano, M. and Williams, L.T. (1994) The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity. Mol. Cell. Biol., 14, 2675-2685.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2675-2685
    • Klippel, A.1    Escobedo, J.A.2    Hirano, M.3    Williams, L.T.4
  • 27
    • 0028018858 scopus 로고
    • The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-I. Stimulation by insulin and inhibition by wortmannin
    • Lam, K., Carpenter, C.L., Ruderman, N.B., Friel, J.C. and Kelly, K.L. (1994) The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-I. Stimulation by insulin and inhibition by wortmannin. J. Biol. Chem., 269, 20648-20652.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20648-20652
    • Lam, K.1    Carpenter, C.L.2    Ruderman, N.B.3    Friel, J.C.4    Kelly, K.L.5
  • 28
    • 0026687883 scopus 로고
    • Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53
    • Lees-Miller, S.P., Sakaguchi, K., Ullrich, S.J., Appella, E. and Anderson, C.W. (1992) Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53. Mol. Cell. Biol., 12, 5041-5049.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5041-5049
    • Lees-Miller, S.P.1    Sakaguchi, K.2    Ullrich, S.J.3    Appella, E.4    Anderson, C.W.5
  • 29
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit
    • Pleiman, C.M., Hertz, W.M. and Cambier, J.C. (1994) Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science, 263, 1609-1612.
    • (1994) Science , vol.263 , pp. 1609-1612
    • Pleiman, C.M.1    Hertz, W.M.2    Cambier, J.C.3
  • 30
    • 0027193980 scopus 로고
    • Divergent regulation of phosphatidylinositol 3-kinase P85 α and P85 β isoforms upon T cell activation
    • Reif, K., Gout, I., Waterfield, M.D. and Cantrell, D.A. (1993) Divergent regulation of phosphatidylinositol 3-kinase P85 α and P85 β isoforms upon T cell activation. J. Biol. Chem., 268, 10780-10788.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10780-10788
    • Reif, K.1    Gout, I.2    Waterfield, M.D.3    Cantrell, D.A.4
  • 31
    • 0029990003 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation
    • Rodriguez-Viciana, P., Warne, P.H., Vanhaesebroeck, B., Waterfield, M.D. and Downward, J. (1996) Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. EMBO J., 15, 2442-2451.
    • (1996) EMBO J. , vol.15 , pp. 2442-2451
    • Rodriguez-Viciana, P.1    Warne, P.H.2    Vanhaesebroeck, B.3    Waterfield, M.D.4    Downward, J.5
  • 33
    • 0030657770 scopus 로고    scopus 로고
    • Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements
    • Schinkmann, K. and Blenis, J. (1997) Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements. J. Biol. Chem., 272, 28695-28703.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28695-28703
    • Schinkmann, K.1    Blenis, J.2
  • 34
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • Shepherd, P.R., Withers, D.J. and Siddle, K. (1998) Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. Biochem. J., 333, 471-190.
    • (1998) Biochem. J. , vol.333 , pp. 471-1190
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 35
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S.Y., Ikeda, M., Taya, Y. and Prives, C. (1997) DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell, 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 36
    • 0028110018 scopus 로고
    • Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities
    • Stack, J.H. and Emr, S.D. (1994) Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities. J. Biol. Chem., 269, 31552-31562.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31552-31562
    • Stack, J.H.1    Emr, S.D.2
  • 37
    • 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. (1993) Agonist-stimulated synthesis of phosphatidylinositol (3,4,5)-trisphosphate: a new intracellular signalling system? Biochim. Biophys. Acta, 1179, 27-75.
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 27-75
    • Stephens, L.R.1    Jackson, T.R.2    Hawkins, P.T.3
  • 38
    • 0030920653 scopus 로고    scopus 로고
    • Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase γ: Structure-activity analysis and interactions with wortmannin
    • Stoyanova, S., Bulgarelli-Leva, G., Kirsch, C., Hanck, T., Klinger, R., Wetzker, R. and Wymann, M.P. (1997) Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase γ: structure-activity analysis and interactions with wortmannin. Biochem. J., 324, 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
  • 39
    • 0027967958 scopus 로고
    • Insulin receptor substrate 1 is phosphorylated by the serine kinase activity of phosphatidylinositol 3-kinase
    • Tanti, J.F., Gremeaux, T., Van Obberghen, E. and Le Marchand-Brustel, Y. (1994) Insulin receptor substrate 1 is phosphorylated by the serine kinase activity of phosphatidylinositol 3-kinase. Biochem. J., 304, 17-21.
    • (1994) Biochem. J. , vol.304 , pp. 17-21
    • Tanti, J.F.1    Gremeaux, T.2    Van Obberghen, E.3    Le Marchand-Brustel, Y.4
  • 40
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A. and Cantley, L.C. (1997) Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature, 387, 673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 42
    • 0029060259 scopus 로고
    • Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion
    • Ueda, Y., Levine, B.L., Huang, M.L., Freeman, G.J., Nadler, L.M., June, C.H. and Ward, S.G. (1995) Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion. Int. Immunol., 7, 957-966.
    • (1995) Int. Immunol. , vol.7 , pp. 957-966
    • Ueda, Y.1    Levine, B.L.2    Huang, M.L.3    Freeman, G.J.4    Nadler, L.M.5    June, C.H.6    Ward, S.G.7
  • 44
    • 0030611198 scopus 로고    scopus 로고
    • p110δ, a novel phosphoinositide 3-kinase in leukocytes
    • Vanhaesebroeck, B. et al. (1997b) p110δ, a novel phosphoinositide 3-kinase in leukocytes. Proc. Natl Acad. Sci. USA, 94, 4330-4335.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4330-4335
    • Vanhaesebroeck, B.1
  • 46
    • 0029965232 scopus 로고    scopus 로고
    • PI 3-kinase: A pivotal pathway in T-cell activation?
    • Ward, S.G., June, C.H. and Olive, D. (1996) PI 3-kinase: a pivotal pathway in T-cell activation? Immunol. Today, 17, 187-197.
    • (1996) Immunol. Today , vol.17 , pp. 187-197
    • Ward, S.G.1    June, C.H.2    Olive, D.3
  • 47
    • 0027056309 scopus 로고
    • Regulation of phosphoinositide kinases in T cells. Evidence that phosphatidylinositol 3-kinase is not a substrate for T cell antigen receptor-regulated tyrosine kinases
    • Ward, S.G., Reif, K., Ley, S., Fry, M.J., Waterfield, M.D. and Cantrell, D.A. (1992) Regulation of phosphoinositide kinases in T cells. Evidence that phosphatidylinositol 3-kinase is not a substrate for T cell antigen receptor-regulated tyrosine kinases. J. Biol. Chem., 267, 23862-23869.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23862-23869
    • Ward, S.G.1    Reif, K.2    Ley, S.3    Fry, M.J.4    Waterfield, M.D.5    Cantrell, D.A.6
  • 48
    • 0027429761 scopus 로고
    • Ligation of CD28 receptor by B7 induces formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation
    • Ward, S.G., Westwick, J., Hall, N.D. and Sansom, D.M. (1993) Ligation of CD28 receptor by B7 induces formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation. Eur. J. Immunol., 23, 2572-2577.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2572-2577
    • Ward, S.G.1    Westwick, J.2    Hall, N.D.3    Sansom, D.M.4
  • 49
    • 0030911015 scopus 로고    scopus 로고
    • p60 is an adaptor for the Drosophila phosphoinositide 3-kinase, Dp110
    • Weinkove, D., Leevers, S.J., MacDougall, L.K. and Waterfield, M.D. (1997) p60 is an adaptor for the Drosophila phosphoinositide 3-kinase, Dp110. J. Biol. Chem., 272, 14606-14610.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14606-14610
    • Weinkove, D.1    Leevers, S.J.2    Macdougall, L.K.3    Waterfield, M.D.4
  • 50
    • 0028021690 scopus 로고
    • Interleukin-4-dependent proliferation dissociates p44erk-1, p42erk-2 and p21ras activation from cell growth
    • Welham, M.J., Duronio, V. and Schrader, J.W. (1994) Interleukin-4-dependent proliferation dissociates p44erk-1, p42erk-2 and p21ras activation from cell growth. J. Biol. Chem., 269, 5865-5873.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5865-5873
    • Welham, M.J.1    Duronio, V.2    Schrader, J.W.3
  • 52
    • 0032514485 scopus 로고    scopus 로고
    • DNA-dependent protein kinase acts upstream of p53 in response to DNA damage
    • Woo, R.A., McLure, K.G., Lees-Miller, S.P., Rancourt, D.E. and Lee, P.W. (1998) DNA-dependent protein kinase acts upstream of p53 in response to DNA damage. Nature, 394, 700-704.
    • (1998) Nature , vol.394 , pp. 700-704
    • Woo, R.A.1    McLure, K.G.2    Lees-Miller, S.P.3    Rancourt, D.E.4    Lee, P.W.5
  • 53
    • 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. (1994) A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase. FEBS Lett., 342, 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
  • 54
    • 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. (1996) Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol., 16, 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
  • 55
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann, M.P. and Pirola, L. (1998) Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta, 1436, 127-150.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 56
    • 0031887249 scopus 로고    scopus 로고
    • Regulation of the p85/p110 phosphatidylinositol 3′-kinase: Stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit
    • Yu, J., Zhang, Y., McIlroy, J., Rordorf-Nikolic, T., Orr, G.A. and Backer, J.M. (1998) Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol., 18, 1379-1387.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1379-1387
    • Yu, J.1    Zhang, Y.2    McIlroy, J.3    Rordorf-Nikolic, T.4    Orr, G.A.5    Backer, J.M.6
  • 57
    • 0030605392 scopus 로고    scopus 로고
    • Structural and functional diversity of phosphoinositide 3-kinases
    • Zvelebil, M.J. et al. (1996) Structural and functional diversity of phosphoinositide 3-kinases. Philos. Trans. R. Soc. Land. B Biol. Sci., 351, 217-223.
    • (1996) Philos. Trans. R. Soc. Land. B Biol. Sci. , vol.351 , pp. 217-223
    • Zvelebil, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.