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Volumn 37, Issue 4, 2009, Pages 615-626

Form and flexibility in phosphoinositide 3-kinases

Author keywords

Cancer; P110; P85; Phosphoinositide 3,4,5 trisphosphate; Phosphoinositide 3 kinase (PI3K)

Indexed keywords

PHOSPHATIDYLINOSITOL 3 KINASE; POLYPHOSPHOINOSITIDE;

EID: 70349335444     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0370615     Document Type: Article
Times cited : (63)

References (110)
  • 1
    • 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. (1999) Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature 402, 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
  • 4
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C. (2002) The phosphoinositide 3-kinase pathway. Science 296, 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 7
    • 55649084906 scopus 로고    scopus 로고
    • Ciraolo, E., Iezzi, M., Marone, R., Marengo, S., Curcio, C., Costa, C., Azzolino, O., Gonella, C., Rubinetto, C., Wu, H. et al. (2008) Phosphoinositide 3-kinase p110β activity: key role in metabolism and mammary gland cancer but not development. Sci. Signaling 1, ra3
    • Ciraolo, E., Iezzi, M., Marone, R., Marengo, S., Curcio, C., Costa, C., Azzolino, O., Gonella, C., Rubinetto, C., Wu, H. et al. (2008) Phosphoinositide 3-kinase p110β activity: key role in metabolism and mammary gland cancer but not development. Sci. Signaling 1, ra3
  • 10
    • 52049091239 scopus 로고    scopus 로고
    • The multiple roles of phosphoinositide 3-kinase in mast cell biology
    • Kim, M.S., Radinger, M. and Gilfillan, A.M. (2008) The multiple roles of phosphoinositide 3-kinase in mast cell biology. Trends Immunol. 29, 493-501
    • (2008) Trends Immunol , vol.29 , pp. 493-501
    • Kim, M.S.1    Radinger, M.2    Gilfillan, A.M.3
  • 11
    • 0034635221 scopus 로고    scopus 로고
    • Roles of PLC-2 and -3 and PI3K in chemoattractant-mediated signal transduction
    • Li, Z., Jiang, H., Xie, W., Zhang, Z., Smrcka, A.V. and Wu, D. (2000) Roles of PLC-2 and -3 and PI3K in chemoattractant-mediated signal transduction. Science 287, 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
  • 14
    • 50849122062 scopus 로고    scopus 로고
    • The p110γ isoform of phosphatidylinositol 3-kinase regulates migration of effector CD4 T lymphocytes into peripheral inflammatory sites
    • Thomas, M.S., Mitchell, J.S., DeNucci, C.C., Martin, A.L. and Shimizu, Y. (2008) The p110γ isoform of phosphatidylinositol 3-kinase regulates migration of effector CD4 T lymphocytes into peripheral inflammatory sites. J. Leukocyte Biol. 84, 814-823
    • (2008) J. Leukocyte Biol , vol.84 , pp. 814-823
    • Thomas, M.S.1    Mitchell, J.S.2    DeNucci, C.C.3    Martin, A.L.4    Shimizu, Y.5
  • 17
    • 0032514801 scopus 로고    scopus 로고
    • Regulation of the p85/ p110α phosphatidylinositol 3′-kinase: Distinct roles for the N-terminal and C-terminal SH2 domains
    • Yu, J., Wjasow, C. and Backer, J.M. (1998) Regulation of the p85/ p110α phosphatidylinositol 3′-kinase: distinct roles for the N-terminal and C-terminal SH2 domains. J. Biol. Chem. 273, 30199-30203
    • (1998) J. Biol. Chem , vol.273 , pp. 30199-30203
    • Yu, J.1    Wjasow, C.2    Backer, J.M.3
  • 19
    • 0030869757 scopus 로고    scopus 로고
    • Heterodimeric phosphoinositide 3-kinase consisting of p85 and p110β is synergistically activated by the βγ subunits of G proteins and phosphotyrosyl peptide
    • Kurosu, H., Maehama, T., Okada, T., Yamamoto, T., Hoshino, S., Fukui, Y., Ui, M., Hazeki, O. and Katada, T. (1997) Heterodimeric phosphoinositide 3-kinase consisting of p85 and p110β is synergistically activated by the βγ subunits of G proteins and phosphotyrosyl peptide. J. Biol. Chem. 272, 24252-24256
    • (1997) J. Biol. Chem , vol.272 , pp. 24252-24256
    • Kurosu, H.1    Maehama, T.2    Okada, T.3    Yamamoto, T.4    Hoshino, S.5    Fukui, Y.6    Ui, M.7    Hazeki, O.8    Katada, T.9
  • 20
    • 0032828890 scopus 로고    scopus 로고
    • Roles of non-catalytic subunits in Gβγ,-induced activation of class I phosphoinositide 3-kinase isoforms β and γ
    • Maier, U., Babich, A. and Nurnberg, B. (1999) Roles of non-catalytic subunits in Gβγ,-induced activation of class I phosphoinositide 3-kinase isoforms β and γ. J. Biol. Chem. 274, 29311-29317
    • (1999) J. Biol. Chem , vol.274 , pp. 29311-29317
    • Maier, U.1    Babich, A.2    Nurnberg, B.3
  • 24
    • 15744363780 scopus 로고    scopus 로고
    • p84, a new Gβγ-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110γ
    • Suire, S., Coadwell, J., Ferguson, G.J., Davidson, K., Hawkins, P. and Stephens, L. (2005) p84, a new Gβγ-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110γ. Curr. Biol. 15, 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
  • 25
    • 33744518663 scopus 로고    scopus 로고
    • Characterization of p87PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase γ that is highly expressed in heart and interacts with PDE3B
    • Voigt, P., Dorner, M.B. and Schaefer, M. (2006) Characterization of p87PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase γ that is highly expressed in heart and interacts with PDE3B. J. Biol. Chem. 281, 9977-9986
    • (2006) J. Biol. Chem , vol.281 , pp. 9977-9986
    • Voigt, P.1    Dorner, M.B.2    Schaefer, M.3
  • 26
    • 14244266719 scopus 로고    scopus 로고
    • Assigning functional domains within the p101 regulatory subunit of phosphoinositide 3-kinase γ
    • Voigt, P., Brock, C., Nurnberg, B. and Schaefer, M. (2005) Assigning functional domains within the p101 regulatory subunit of phosphoinositide 3-kinase γ. J. Biol. Chem. 280, 5121-5127
    • (2005) J. Biol. Chem , vol.280 , pp. 5121-5127
    • Voigt, P.1    Brock, C.2    Nurnberg, B.3    Schaefer, M.4
  • 27
    • 35548991099 scopus 로고    scopus 로고
    • Overexpression of p101 activates PI3Kγ signaling in T cells and contributes to cell survival
    • Johnson, C., Marriott, S.J. and Levy, L.S. (2007) Overexpression of p101 activates PI3Kγ signaling in T cells and contributes to cell survival. Oncogene 26, 7049-7057
    • (2007) Oncogene , vol.26 , pp. 7049-7057
    • Johnson, C.1    Marriott, S.J.2    Levy, L.S.3
  • 29
    • 0037086679 scopus 로고    scopus 로고
    • Mechanism of the regulation of type IB phosphoinositide 3OH-kinase by G-protein βγ subunits
    • Krugmann, S., Cooper, M.A., Williams, D.H., Hawkins, P.T. and Stephens, L.R. (2002) Mechanism of the regulation of type IB phosphoinositide 3OH-kinase by G-protein βγ subunits. Biochem. J. 362, 725-731
    • (2002) Biochem. J , vol.362 , pp. 725-731
    • Krugmann, S.1    Cooper, M.A.2    Williams, D.H.3    Hawkins, P.T.4    Stephens, L.R.5
  • 30
    • 54849438886 scopus 로고    scopus 로고
    • 3 formation monitored by a fluorescent Gβγ biosensor protein and repetitive two component total internal reflection/fluorescence redistribution after photobleaching analysis
    • 3 formation monitored by a fluorescent Gβγ biosensor protein and repetitive two component total internal reflection/fluorescence redistribution after photobleaching analysis. Biochemistry 47, 11239-11250
    • (2008) Biochemistry , vol.47 , pp. 11239-11250
    • Tannert, A.1    Voigt, P.2    Burgold, S.3    Tannert, S.4    Schaefer, M.5
  • 31
    • 34247141906 scopus 로고    scopus 로고
    • Role of class II phosphoinositide 3-kinase in cell signalling
    • Falasca, M. and Maffucci, T. (2007) Role of class II phosphoinositide 3-kinase in cell signalling. Biochem. Soc. Trans. 35, 211-214
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 211-214
    • Falasca, M.1    Maffucci, T.2
  • 32
    • 0035103107 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2α is activated by clathrin and regulates clathrin-mediated membrane trafficking
    • Gaidarov, I., Smith, M.E., Domin, J. and Keen, J.H. (2001) The class II phosphoinositide 3-kinase C2α is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol. Cell 7, 443-449
    • (2001) Mol. Cell , vol.7 , pp. 443-449
    • Gaidarov, I.1    Smith, M.E.2    Domin, J.3    Keen, J.H.4
  • 33
    • 59449105295 scopus 로고    scopus 로고
    • 2+-regulated pool of phosphatidylinositol 3-phosphate produced by phosphatidylinositol 3-kinase C2α on neurosecretory vesicles
    • 2+-regulated pool of phosphatidylinositol 3-phosphate produced by phosphatidylinositol 3-kinase C2α on neurosecretory vesicles. Mol. Biol. Cell 19, 5593-5603
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5593-5603
    • Wen, P.J.1    Osborne, S.L.2    Morrow, I.C.3    Parton, R.G.4    Domin, J.5    Meunier, F.A.6
  • 34
    • 26244461921 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase C2α is essential for ATP-dependent priming of neurosecretory granule exocytosis
    • Meunier, F.A., Osborne, S.L., Hammond, G.R., Cooke, F.T., Parker, P.J., Domin, J. and Schiavo, G. (2005) Phosphatidylinositol 3-kinase C2α is essential for ATP-dependent priming of neurosecretory granule exocytosis. Mol. Biol. Cell 16, 4841-4851
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4841-4851
    • Meunier, F.A.1    Osborne, S.L.2    Hammond, G.R.3    Cooke, F.T.4    Parker, P.J.5    Domin, J.6    Schiavo, G.7
  • 37
    • 0033591247 scopus 로고    scopus 로고
    • Insulin activates the α isoform of class II phosphoinositide 3-kinase
    • Brown, R.A., Domin, J., Arcaro, A., Waterfield, M.D. and Shepherd, P.R. (1999) Insulin activates the α isoform of class II phosphoinositide 3-kinase. J. Biol. Chem. 274, 14529-14532
    • (1999) J. Biol. Chem , vol.274 , pp. 14529-14532
    • Brown, R.A.1    Domin, J.2    Arcaro, A.3    Waterfield, M.D.4    Shepherd, P.R.5
  • 38
    • 0035893287 scopus 로고    scopus 로고
    • Class II phosphoinositide 3-kinase is activated by insulin but not by contraction in skeletal muscle
    • Soos, M.A., Jensen, J., Brown, R.A., O'Rahilly, S., Shepherd, P.R. and Whitehead, J.P. (2001) Class II phosphoinositide 3-kinase is activated by insulin but not by contraction in skeletal muscle. Arch. Biochem. Biophys. 396, 244-248
    • (2001) Arch. Biochem. Biophys , vol.396 , pp. 244-248
    • Soos, M.A.1    Jensen, J.2    Brown, R.A.3    O'Rahilly, S.4    Shepherd, P.R.5    Whitehead, J.P.6
  • 39
    • 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. (2005) Class II phosphoinositide 3-kinase defines a novel signaling pathway in cell migration. J. Cell Biol. 169, 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
  • 40
    • 27744606985 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase PI3K-C2β regulates cell migration by a PtdIns3P dependent mechanism
    • Domin, J., Harper, L., Aubyn, D., Wheeler, M., Florey, O., Haskard, D., Yuan, M. and Zicha, D. (2005) The class II phosphoinositide 3-kinase PI3K-C2β regulates cell migration by a PtdIns3P dependent mechanism. J. Cell Physiol. 205, 452-462
    • (2005) J. Cell Physiol , vol.205 , pp. 452-462
    • Domin, J.1    Harper, L.2    Aubyn, D.3    Wheeler, M.4    Florey, O.5    Haskard, D.6    Yuan, M.7    Zicha, D.8
  • 43
    • 31944448792 scopus 로고    scopus 로고
    • The N-terminus of phosphoinositide 3-kinase-C2β regulates lipid kinase activity and binding to clathrin
    • Wheeler, M. and Domin, J. (2006) The N-terminus of phosphoinositide 3-kinase-C2β regulates lipid kinase activity and binding to clathrin. J. Cell. Physiol. 206, 586-593
    • (2006) J. Cell. Physiol , vol.206 , pp. 586-593
    • Wheeler, M.1    Domin, J.2
  • 44
  • 45
    • 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. (2006) The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7, 606-619
    • (2006) Nat. Rev. Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 46
    • 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. (1993) Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260, 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
  • 47
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown, W.J., DeWald, D.B., Emr, S.D., Plutner, H. and Balch, W.E. (1995) Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130, 781-796
    • (1995) J. Cell Biol , vol.130 , pp. 781-796
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 48
    • 39749141485 scopus 로고    scopus 로고
    • The regulation and function of Class III PI3Ks: Novel roles for Vps34
    • Backer, J.M. (2008) The regulation and function of Class III PI3Ks: novel roles for Vps34. Biochem. J. 410, 1-17
    • (2008) Biochem. J , vol.410 , pp. 1-17
    • Backer, J.M.1
  • 49
    • 34247120977 scopus 로고    scopus 로고
    • Nutrient sensing in the mTOR/S6K1 signalling pathway
    • Gulati, P. and Thomas, G. (2007) Nutrient sensing in the mTOR/S6K1 signalling pathway. Biochem. Soc. Trans. 35, 236-238
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 236-238
    • Gulati, P.1    Thomas, G.2
  • 51
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield, M.P., Murray, J.T. and Backer, J.M. (2005) hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J. Biol. Chem. 280, 33076-33082
    • (2005) J. Biol. Chem , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 52
    • 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. (2001) Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152, 519-530
    • (2001) J. Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 53
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura, E., Kishi, C., Inoue, K. and Mizushima, N. (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol. Biol. Cell 19, 5360-5372
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 54
    • 58049192897 scopus 로고    scopus 로고
    • Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • Sun, Q., Fan, W., Chen, K., Ding, X., Chen, S. and Zhong, Q. (2008) Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. U.S.A. 105, 19211-19216
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 19211-19216
    • Sun, Q.1    Fan, W.2    Chen, K.3    Ding, X.4    Chen, S.5    Zhong, Q.6
  • 55
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • Liang, C., Feng, P., Ku, B., Dotan, I., Canaani, D., Oh, B.H. and Jung, J.U. (2006) Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat. Cell Biol. 8, 688-699
    • (2006) Nat. Cell Biol , vol.8 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3    Dotan, I.4    Canaani, D.5    Oh, B.H.6    Jung, J.U.7
  • 58
    • 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
  • 60
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M. and Kuriyan, J. (2002) The conformational plasticity of protein kinases. Cell 109, 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 61
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu, Y. and Gray, N.S. (2006) Rational design of inhibitors that bind to inactive kinase conformations. Nat. Chem. Biol. 2, 358-364
    • (2006) Nat. Chem. Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 63
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase δ in neutrophil directional movement
    • Sadhu, C., Masinovsky, B., Dick, K., Sowell, C.G. and Staunton, D.E. (2003) Essential role of phosphoinositide 3-kinase δ in neutrophil directional movement. J. Immunol. 170, 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
  • 68
    • 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. (2000) Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6, 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
  • 69
    • 52449106253 scopus 로고    scopus 로고
    • Folkes, A.J., Ahmadi, K., Alderton, W.K., Alix, S., Baker, S.J., Box, G., Chuckowree, I.S., Clarke, P.A., Depledge, P., Eccles, S.A. et al. (2008) The identification of 2-(1H-indazol-4-yl)-6-(4-methanesulfonyl-piperazin- 1-ylmethyl)-4-morpholin-4-yl-thieno[3,2-d]pyrimidine (GDC-0941) as a potent, selective, orally bioavailable inhibitor of class I PI3 kinase for the treatment of cancer. J. Med. Chem. 51, 5522-5532
    • Folkes, A.J., Ahmadi, K., Alderton, W.K., Alix, S., Baker, S.J., Box, G., Chuckowree, I.S., Clarke, P.A., Depledge, P., Eccles, S.A. et al. (2008) The identification of 2-(1H-indazol-4-yl)-6-(4-methanesulfonyl-piperazin- 1-ylmethyl)-4-morpholin-4-yl-thieno[3,2-d]pyrimidine (GDC-0941) as a potent, selective, orally bioavailable inhibitor of class I PI3 kinase for the treatment of cancer. J. Med. Chem. 51, 5522-5532
  • 70
    • 44649150564 scopus 로고    scopus 로고
    • Structure-based design of an organoruthenium phosphatidyl-inositol-3-kinase inhibitor reveals a switch governing lipid kinase potency and selectivity. ACS
    • Xie, P., Williams, D.S., Atilla-Gokcumen, G.E., Milk, L., Xiao, M., Smalley, K.S., Herlyn, M., Meggers, E. and Marmorstein, R. (2008) Structure-based design of an organoruthenium phosphatidyl-inositol-3-kinase inhibitor reveals a switch governing lipid kinase potency and selectivity. ACS Chem. Biol. 3, 305-316
    • (2008) Chem. Biol , vol.3 , pp. 305-316
    • Xie, P.1    Williams, D.S.2    Atilla-Gokcumen, G.E.3    Milk, L.4    Xiao, M.5    Smalley, K.S.6    Herlyn, M.7    Meggers, E.8    Marmorstein, R.9
  • 74
    • 33644787284 scopus 로고    scopus 로고
    • Study on improving the selectivity of compounds that inhibit two PI3Ks (γ and δ)
    • Kuang, R.R., Qian, F., Li, Z. and Wei, D.Z. (2006) Study on improving the selectivity of compounds that inhibit two PI3Ks (γ and δ). J. Mol. Model. 12, 445-452
    • (2006) J. Mol. Model , vol.12 , pp. 445-452
    • Kuang, R.R.1    Qian, F.2    Li, Z.3    Wei, D.Z.4
  • 75
    • 33646147812 scopus 로고    scopus 로고
    • Action mechanisms and structure-activity relationships of PI3Kγ inhibitors on the enzyme: A molecular modeling study
    • Kuang, R.R., Qian, F., Li, Z., Wei, D.Z. and Tang, Y. (2006) Action mechanisms and structure-activity relationships of PI3Kγ inhibitors on the enzyme: a molecular modeling study. Eur. J. Med. Chem. 41, 558-565
    • (2006) Eur. J. Med. Chem , vol.41 , pp. 558-565
    • Kuang, R.R.1    Qian, F.2    Li, Z.3    Wei, D.Z.4    Tang, Y.5
  • 77
    • 51849128358 scopus 로고    scopus 로고
    • Class I PI3K in oncogenic cellular transformation
    • Zhao, L. and Vogt, P.K. (2008) Class I PI3K in oncogenic cellular transformation. Oncogene 27, 5486-5496
    • (2008) Oncogene , vol.27 , pp. 5486-5496
    • Zhao, L.1    Vogt, P.K.2
  • 79
    • 33646706052 scopus 로고    scopus 로고
    • Oncogenic PI3K and its role in cancer
    • Samuels, Y. and Ericson, K. (2006) Oncogenic PI3K and its role in cancer. Curr. Opin. Oncol. 18, 77-82
    • (2006) Curr. Opin. Oncol , vol.18 , pp. 77-82
    • Samuels, Y.1    Ericson, K.2
  • 81
    • 31944444234 scopus 로고    scopus 로고
    • Cancer-specific mutations in PIK3CA are oncogenic in vivo
    • Bader, A.G., Kang, S. and Vogt, P.K. (2006) Cancer-specific mutations in PIK3CA are oncogenic in vivo. Proc. Natl. Acad. Sci. U.S.A. 103, 1475-1479
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 1475-1479
    • Bader, A.G.1    Kang, S.2    Vogt, P.K.3
  • 82
    • 54549108740 scopus 로고    scopus 로고
    • Comprehensive genomic characterization defines human glioblastoma genes and core pathways
    • Cancer Genome Atlas Research Network
    • Cancer Genome Atlas Research Network (2008) Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 455, 1061-1068
    • (2008) Nature , vol.455 , pp. 1061-1068
  • 84
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang, S., Bader, A.G. and Vogt, P.K. (2005) Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc. Natl. Acad. Sci. U.S.A. 102, 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
  • 86
    • 34248369435 scopus 로고    scopus 로고
    • Rare cancer-specific mutations in PIK3CA show gain of function
    • Gymnopoulos, M., Elsliger, M.A. and Vogt, P.K. (2007) Rare cancer-specific mutations in PIK3CA show gain of function. Proc. Natl. Acad. Sci. U.S.A. 104, 5569-5574
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 5569-5574
    • Gymnopoulos, M.1    Elsliger, M.A.2    Vogt, P.K.3
  • 88
    • 66149100073 scopus 로고    scopus 로고
    • PIK3CA somatic mutations in breast cancer: Mechanistic insights from Langevin dynamics simulations
    • Mankoo, P.K., Sukumar, S. and Karchin, R. (2009) PIK3CA somatic mutations in breast cancer: mechanistic insights from Langevin dynamics simulations. Proteins 75, 499-508
    • (2009) Proteins , vol.75 , pp. 499-508
    • Mankoo, P.K.1    Sukumar, S.2    Karchin, R.3
  • 90
    • 40649096375 scopus 로고    scopus 로고
    • Helical domain and kinase domain mutations in p110α of phosphatidylinositol 3-kinase induce gain of function by different mechanisms
    • Zhao, L. and Vogt, P.K. (2008) Helical domain and kinase domain mutations in p110α of phosphatidylinositol 3-kinase induce gain of function by different mechanisms. Proc. Natl. Acad. Sci. U.S.A. 105, 2652-2657
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 2652-2657
    • Zhao, L.1    Vogt, P.K.2
  • 93
    • 33750459743 scopus 로고    scopus 로고
    • A selective inhibitor of the p110d 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. (2006) A selective inhibitor of the p110d isoform of PI 3-kinase inhibits AML cell proliferation and survival and increases the cytotoxic effects of VP16. Oncogene 25, 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
  • 94
    • 31944448780 scopus 로고    scopus 로고
    • Oncogenic transformation induced by the p110β, γ, and -δ isoforms of class I phosphoinositide 3-kinase
    • Kang, S., Denley, A., Vanhaesebroeck, B. and Vogt, P.K. (2006) Oncogenic transformation induced by the p110β, γ, and -δ isoforms of class I phosphoinositide 3-kinase. Proc. Natl. Acad. Sci. U.S.A. 103, 1289-1294
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 1289-1294
    • Kang, S.1    Denley, A.2    Vanhaesebroeck, B.3    Vogt, P.K.4
  • 98
    • 50149101312 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibitors: Promising drug candidates for cancer therapy
    • Kong, D. and Yamori, T. (2008) Phosphatidylinositol 3-kinase inhibitors: promising drug candidates for cancer therapy. Cancer Sci. 99, 1734-1740
    • (2008) Cancer Sci , vol.99 , pp. 1734-1740
    • Kong, D.1    Yamori, T.2
  • 99
    • 58149509984 scopus 로고    scopus 로고
    • Take your PIK: Phosphatidylinositol 3-kinase inhibitors race through the clinic and toward cancer therapy
    • Ihle, N.T. and Powis, G. (2009) Take your PIK: phosphatidylinositol 3-kinase inhibitors race through the clinic and toward cancer therapy. Mol. Cancer Ther. 8, 1-9
    • (2009) Mol. Cancer Ther , vol.8 , pp. 1-9
    • Ihle, N.T.1    Powis, G.2
  • 101
    • 50149115138 scopus 로고    scopus 로고
    • Structural analysis of PI3-kinase isoforms: Identification of residues enabling selective inhibition by small molecule ATP-competitive inhibitors
    • Zvelebil, M.J., Waterfield, M.D. and Shuttleworth, S.J. (2008) Structural analysis of PI3-kinase isoforms: identification of residues enabling selective inhibition by small molecule ATP-competitive inhibitors. Arch. Biochem. Biophys. 477, 404-410
    • (2008) Arch. Biochem. Biophys , vol.477 , pp. 404-410
    • Zvelebil, M.J.1    Waterfield, M.D.2    Shuttleworth, S.J.3
  • 104
    • 0036185944 scopus 로고    scopus 로고
    • Early embryonic lethality in mice deficient in the p110β catalytic subunit of PI 3-kinase
    • Bi, L., Okabe, I., Bernard, D.J. and Nussbaum, R.L. (2002) Early embryonic lethality in mice deficient in the p110β catalytic subunit of PI 3-kinase. Mamm. Genome 13, 169-172
    • (2002) Mamm. Genome , vol.13 , pp. 169-172
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Nussbaum, R.L.4
  • 109
    • 38549099762 scopus 로고    scopus 로고
    • Dynamic regulation of phosphoinositide 3-kinase-γ activity and β-adrenergic receptor trafficking in end-stage human heart failure
    • Perrino, C., Schroder, J.N., Lima, B., Villamizar, N., Nienaber, J.J., Milano, C.A. and Naga Prasad, S.V. (2007) Dynamic regulation of phosphoinositide 3-kinase-γ activity and β-adrenergic receptor trafficking in end-stage human heart failure. Circulation 116, 2571-2579
    • (2007) Circulation , vol.116 , pp. 2571-2579
    • Perrino, C.1    Schroder, J.N.2    Lima, B.3    Villamizar, N.4    Nienaber, J.J.5    Milano, C.A.6    Naga Prasad, S.V.7
  • 110
    • 85047693926 scopus 로고    scopus 로고
    • Inhibition of receptor-localized PI3K preserves cardiac β-adrenergic receptor function and ameliorates pressure overload heart failure
    • Nienaber, J.J., Tachibana, H., Naga Prasad, S.V., Esposito, G., Wu, D., Mao, L. and Rockman, H.A. (2003) Inhibition of receptor-localized PI3K preserves cardiac β-adrenergic receptor function and ameliorates pressure overload heart failure. J. Clin. Invest. 112, 1067-1079
    • (2003) J. Clin. Invest , vol.112 , pp. 1067-1079
    • Nienaber, J.J.1    Tachibana, H.2    Naga Prasad, S.V.3    Esposito, G.4    Wu, D.5    Mao, L.6    Rockman, H.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.