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Volumn 11, Issue , 2011, Pages

Inositol pentakisphosphate isomers bind PH domains with varying specificity and inhibit phosphoinositide interactions

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL PENTAKISPHOSPHATE; PHOSPHATIDYLINOSITIDE; PLECKSTRIN; PROTEIN KINASE B; CELL RECEPTOR; INOSITOL PHOSPHATE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL RECEPTORS; PHOSPHOPROTEIN; PLASMA PROTEIN; PLATELET PROTEIN P47; SIGNAL PEPTIDE;

EID: 79751535258     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-11     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 33644877451 scopus 로고    scopus 로고
    • SMART 5: Domains in the context of genomes and networks
    • 10.1093/nar/gkj079. 16381859
    • SMART 5: domains in the context of genomes and networks. I Letunic RR Copley B Pils S Pinkert J Schultz P Bork, Nucleic Acids Res 2006 34 Database 257 60 10.1093/nar/gkj079 16381859
    • (2006) Nucleic Acids Res , Issue.34 DATABASE , pp. 4257-60
    • Letunic, I.1    Copley, R.R.2    Pils, B.3    Pinkert, S.4    Schultz, J.5    Bork, P.6
  • 3
    • 0033634785 scopus 로고    scopus 로고
    • Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains
    • 10.1016/S1097-2765(00)00038-1. 10983985
    • Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains. SE Lietzke S Bose T Cronin J Klarlund A Chawla P Czech DG Lambright, Mol Cell 2000 6 2 385 10.1016/S1097-2765(00)00038-1 10983985
    • (2000) Mol Cell , vol.6 , Issue.2 , pp. 385
    • Lietzke, S.E.1    Bose, S.2    Cronin, T.3    Klarlund, J.4    Chawla, A.5    Czech, P.6    Lambright, D.G.7
  • 4
    • 0033635275 scopus 로고    scopus 로고
    • Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains
    • 10.1016/S1097-2765(00)00037-X. 10983984
    • Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains. KM Ferguson JM Kavran VG Sankaran E Fournier SJ Isakoff EY Skolnik MA Lemmon, Mol Cell 2000 6 2 373 384 10.1016/S1097-2765(00)00037-X 10983984
    • (2000) Mol Cell , vol.6 , Issue.2 , pp. 373-384
    • Ferguson, K.M.1    Kavran, J.M.2    Sankaran, V.G.3    Fournier, E.4    Isakoff, S.J.5    Skolnik, E.Y.6    Lemmon, M.A.7
  • 5
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • DOI 10.1038/371168a0
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5- bisphosphate. JE Harl (Pubitemid 24284017)
    • (1994) Nature , vol.371 , Issue.6493 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 6
    • 0029087181 scopus 로고
    • Structural characterization of the interaction between a pleckstrin homology domain and phosphatidylinositol 4,5-bisphosphate
    • 10.1021/bi00031a006. 7632686
    • Structural characterization of the interaction between a pleckstrin homology domain and phosphatidylinositol 4,5-bisphosphate. JE Harlan HS Yoon PJ Hajduk SW Fesik, Biochemistry 1995 34 31 9859 9864 10.1021/bi00031a006 7632686
    • (1995) Biochemistry , vol.34 , Issue.31 , pp. 9859-9864
    • Harlan, J.E.1    Yoon, H.S.2    Hajduk, P.J.3    Fesik, S.W.4
  • 7
    • 69249090082 scopus 로고    scopus 로고
    • Phosphoinositide Signaling: New Tools and Insights
    • 10.1152/physiol.00014.2009. 19675354
    • Phosphoinositide Signaling: New Tools and Insights. T Balla Y Szentpetery J Kim, Physiology 2009 24 4 231 10.1152/physiol.00014.2009 19675354
    • (2009) Physiology , vol.24 , Issue.4 , pp. 231
    • Balla, T.1    Szentpetery, Y.2    Kim, J.3
  • 8
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • DOI 10.1038/35073015
    • Back in the water: the return of the inositol phosphates. RF Irvine MJ Schell, Nat Rev Mol Cell Biol 2001 2 5 327 338 10.1038/35073015 11331907 (Pubitemid 33674045)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 10
    • 0023772341 scopus 로고
    • Inositol phosphates: A family of signal molecules?
    • 10.1016/0166-2236(88)90051-3. 2469189
    • Inositol phosphates: a family of signal molecules? CP Downes, Trends Neurosci 1988 11 8 336 10.1016/0166-2236(88)90051-3 2469189
    • (1988) Trends Neurosci , vol.11 , Issue.8 , pp. 336
    • Downes, C.P.1
  • 11
    • 0025187787 scopus 로고
    • Myo-inositol metabolites as cellular signals
    • 10.1111/j.1432-1033.1990.tb19297.x. 2171926
    • myo-inositol metabolites as cellular signals. CP Downes CH Macphee, Eur J Biochem 1990 193 1 10.1111/j.1432-1033.1990.tb19297.x 2171926
    • (1990) Eur J Biochem , vol.193 , Issue.1
    • Downes, C.P.1    MacPhee, C.H.2
  • 12
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • DOI 10.1038/341197a0
    • Inositol phosphates and cell signalling. MJ Berridge RF Irvine, Nature 1989 341 6239 197 205 10.1038/341197a0 2550825 (Pubitemid 19231718)
    • (1989) Nature , vol.341 , Issue.6239 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 15
    • 0033612242 scopus 로고    scopus 로고
    • 2+ mobilization patterns
    • DOI 10.1126/science.284.5419.1527
    • 2+ mobilization patterns. K Hirose S Kadowaki M Tanabe H Takeshima M Iino, Science 1999 283 1527 10.1126/science.284.5419.1527 (Pubitemid 29291399)
    • (1999) Science , vol.284 , Issue.5419 , pp. 1527-1530
    • Hirose, K.1    Kadowaki, S.2    Tanabe, M.3    Takeshima, H.4    Iino, M.5
  • 16
    • 13844253933 scopus 로고    scopus 로고
    • Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin
    • DOI 10.1016/j.str.2004.11.012
    • Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin. C Edlich G Stier B Simon M Sattler C Muhle-Goll, Structure 2005 13 2 277 286 10.1016/j.str.2004.11.012 15698571 (Pubitemid 40247703)
    • (2005) Structure , vol.13 , Issue.2 , pp. 277-286
    • Edlich, C.1    Stier, G.2    Simon, B.3    Sattler, M.4    Muhle-Goll, C.5
  • 17
    • 38349049373 scopus 로고    scopus 로고
    • Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate
    • 18034889
    • Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate. SG Jackson Y Zhang RJ Haslam MS Junop, BMC Structural Biology 2007 7 80 18034889
    • (2007) BMC Structural Biology , vol.7 , Issue.80
    • Jackson, S.G.1    Zhang, Y.2    Haslam, R.J.3    Junop, M.S.4
  • 20
    • 0034113153 scopus 로고    scopus 로고
    • Novel functional PI 3-kinase antagonists inhibit cell growth and tumorigenicity in human cancer cell lines
    • 10834940
    • Novel functional PI 3-kinase antagonists inhibit cell growth and tumorigenicity in human cancer cell lines. G Razzini CP Berrie S Vignati M Broggini G Mascetta A Brancaccio M Falasca, FASEB Journal 2000 14 9 1179 10834940
    • (2000) FASEB Journal , vol.14 , Issue.9 , pp. 1179
    • Razzini, G.1    Berrie, C.P.2    Vignati, S.3    Broggini, M.4    Mascetta, G.5    Brancaccio, A.6    Falasca, M.7
  • 21
    • 34548844487 scopus 로고    scopus 로고
    • Recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors
    • 10.2174/156802607781696864. 17692025
    • Recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors. CW Lindsley BF Stanley M Yaroschak MT Bilodeau ME Layton, Curr Top Med Chem 2007 7 14 1349 10.2174/156802607781696864 17692025
    • (2007) Curr Top Med Chem , vol.7 , Issue.14 , pp. 1349
    • Lindsley, C.W.1    Stanley, B.F.2    Yaroschak, M.3    Bilodeau, M.T.4    Layton, M.E.5
  • 22
    • 39049171769 scopus 로고    scopus 로고
    • The PI3K/Akt pathways: Recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors
    • 10.2174/156800908783497096. 18288939
    • The PI3K/Akt pathways: recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors. CW Lindsley BF Stanley ME Layton MT Bilodeau, Curr Cancer Drug Targets 2008 8 1 7 10.2174/ 156800908783497096 18288939
    • (2008) Curr Cancer Drug Targets , vol.8 , Issue.1 , pp. 7
    • Lindsley, C.W.1    Stanley, B.F.2    Layton, M.E.3    Bilodeau, M.T.4
  • 23
    • 0037333460 scopus 로고    scopus 로고
    • Prodrugs of biologically active phosphate esters
    • 10.1016/S0968-0896(02)00552-7. 12614874
    • Prodrugs of biologically active phosphate esters. C Schultz, Bioorg Med Chem 2003 11 6 885 10.1016/S0968-0896(02)00552-7 12614874
    • (2003) Bioorg Med Chem , vol.11 , Issue.6 , pp. 885
    • Schultz, C.1
  • 24
    • 77951296416 scopus 로고    scopus 로고
    • Activation of membrane-permeant caged PtdIns(3)P induces endosomal fusion in cells
    • 10.1038/nchembio.348. 20364126
    • Activation of membrane-permeant caged PtdIns(3)P induces endosomal fusion in cells. D Subramanian V Laketa R Muller C Tischer S Zarbakhsh R Pepperkok C Schultz, Nat Chem Biol 2010 6 5 324 10.1038/nchembio.348 20364126
    • (2010) Nat Chem Biol , vol.6 , Issue.5 , pp. 324
    • Subramanian, D.1    Laketa, V.2    Muller, R.3    Tischer, C.4    Zarbakhsh, S.5    Pepperkok, R.6    Schultz, C.7
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode. Z Otwinowski W Minor, Methods in Enzymology 1997 276 Macromolecular Crystallography, part A 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • MOLREP: an automated program for molecular replacement. A Vagin A Teplyakov, J Appl Cryst 1997 30 1022 1025 10.1107/S0021889897006766 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 28
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • DOI 10.1107/S0907444904019158
    • Coot: model-building tools for molecular graphics. P Emsley K Cowtan, Acta Crystallogr D Biol Crystallogr 2004 60 Pt 12 Pt 1 2126 2132 10.1107/S0907444904019158 15572765 (Pubitemid 41742764)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.1-12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • 10.1093/bioinformatics/15.4.327. 10320401
    • Automated analysis of interatomic contacts in proteins. V Sobolev A Sorokine J Prilusky EE Abola M Edelman, Bioinformatics 1999 15 327 10.1093/bioinformatics/15.4.327 10320401
    • (1999) Bioinformatics , vol.15 , pp. 327
    • Sobolev, V.1    Sorokine, A.2    Prilusky, J.3    Abola, E.E.4    Edelman, M.5


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