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Volumn 50, Issue 51, 2011, Pages 11143-11161

Phosphatidylinositol 3,4,5-trisphosphate activity probes for the labeling and proteomic characterization of protein binding partners

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY PROBES; BIFUNCTIONAL ACTIVITY; BINDING PROTEINS; BIOLOGICAL PROCESS; CANCER CELLS; CELL EXTRACTS; CLICK CHEMISTRY; COMPLEX SAMPLES; COVALENT LABELING; FLUORESCENT DYES; LABELED PROTEINS; MEMBRANE ASSOCIATION; OPTICAL DETECTION; PHOSPHATIDYLINOSITOL; PHOTOAFFINITY; POLYPHOSPHATES; PROTEIN BINDING PARTNERS; PROTEIN DENATURATION; PROTEIN LABELING; PURIFIED PROTEIN; SITE-SPECIFIC; SYNTHETIC STRATEGIES; TANDEM MASS SPECTROMETRY; TARGET PROTEINS;

EID: 84055193026     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201636s     Document Type: Article
Times cited : (44)

References (92)
  • 1
    • 77957158189 scopus 로고    scopus 로고
    • Inositol polyphosphates, diphosphoinositol polyphosphates and phosphatidylinositol polyphosphate lipids: Structure, synthesis, and development of probes for studying biological activity
    • Best, M. D., Zhang, H. L., and Prestwich, G. D. (2010) Inositol polyphosphates, diphosphoinositol polyphosphates and phosphatidylinositol polyphosphate lipids: Structure, synthesis, and development of probes for studying biological activity Nat. Prod. Rep. 27, 1403-1430
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 1403-1430
    • Best, M.D.1    Zhang, H.L.2    Prestwich, G.D.3
  • 2
    • 34547102761 scopus 로고    scopus 로고
    • Biology-enabling inositol phosphates, phosphatidylinositol phosphates and derivatives
    • DOI 10.1039/b407701f
    • Conway, S. J. and Miller, G. J. (2007) Biology-enabling inositol phosphates, phosphatidylinositol phosphates and derivatives Nat. Prod. Rep. 24, 687-707 (Pubitemid 47106911)
    • (2007) Natural Product Reports , vol.24 , Issue.4 , pp. 687-707
    • Conway, S.J.1    Miller, G.J.2
  • 3
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • DOI 10.1038/nrm2328, PII NRM2328
    • Lemmon, M. A. (2008) Membrane recognition by phospholipid-binding domains Nat. Rev. Mol. Cell Biol. 9, 99-111 (Pubitemid 351158910)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 4
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • DOI 10.1146/annurev.biophys.33.110502.133337
    • Cho, W. and Stahelin, R. V. (2005) Membrane-protein interactions in cell signaling and membrane trafficking Annu. Rev. Biophys. Biomol. Struct. 34, 119-151 (Pubitemid 40847721)
    • (2005) Annual Review of Biophysics and Biomolecular Structure , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 5
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • Di Paolo, G. and De Camilli, P. (2006) Phosphoinositides in cell regulation and membrane dynamics Nature 443, 651-657 (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 6
    • 0038538512 scopus 로고    scopus 로고
    • Phosphoinositide signaling disorders in human diseases
    • DOI 10.1016/S0014-5793(03)00437-X
    • Pendaries, C., Tronchere, H., Plantavid, M., and Payrastre, B. (2003) Phosphoinositide signaling disorders in human diseases FEBS Lett. 546, 25-31 (Pubitemid 36782278)
    • (2003) FEBS Letters , vol.546 , Issue.1 , pp. 25-31
    • Pendaries, C.1    Tronchere, H.2    Plantavid, M.3    Payrastre, B.4
  • 7
    • 52549091027 scopus 로고    scopus 로고
    • Phosphoinositides as regulators of membrane trafficking in health and disease
    • Vicinanza, M., D'Angelo, G., Di Campli, A., and De Matteis, M. A. (2008) Phosphoinositides as regulators of membrane trafficking in health and disease Cell. Mol. Life Sci. 65, 2833-2841
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2833-2841
    • Vicinanza, M.1    D'Angelo, G.2    Di Campli, A.3    De Matteis, M.A.4
  • 9
    • 58249083478 scopus 로고    scopus 로고
    • The TGF-β, PI3K/Akt and PTEN pathways: Established and proposed biochemical integration in prostate cancer
    • Assinder, S. J., Dong, Q. H., Kovacevic, Z., and Richardson, D. R. (2009) The TGF-β, PI3K/Akt and PTEN pathways: Established and proposed biochemical integration in prostate cancer Biochem. J. 417, 411-421
    • (2009) Biochem. J. , vol.417 , pp. 411-421
    • Assinder, S.J.1    Dong, Q.H.2    Kovacevic, Z.3    Richardson, D.R.4
  • 10
    • 58149175555 scopus 로고    scopus 로고
    • The life of a cell: Apoptosis regulation by the PI3K/PKB pathway
    • Duronio, V. (2008) The life of a cell: Apoptosis regulation by the PI3K/PKB pathway Biochem. J. 415, 333-344
    • (2008) Biochem. J. , vol.415 , pp. 333-344
    • Duronio, V.1
  • 11
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • DOI 10.1038/nrg1879, PII NRG1879
    • 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 (Pubitemid 44100518)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.8 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 12
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB Signaling: Navigating Downstream
    • DOI 10.1016/j.cell.2007.06.009, PII S0092867407007751
    • Manning, B. D. and Cantley, L. C. (2007) AKT/PKB signaling: Navigating downstream Cell 129, 1261-1274 (Pubitemid 46962095)
    • (2007) Cell , vol.129 , Issue.7 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 13
    • 43049128529 scopus 로고    scopus 로고
    • Tenets of PTEN Tumor Suppression
    • DOI 10.1016/j.cell.2008.04.013, PII S0092867408005047
    • Salmena, L., Carracedo, A., and Pandolfi, P. P. (2008) Tenets of PTEN tumor suppression Cell 133, 403-414 (Pubitemid 351622014)
    • (2008) Cell , vol.133 , Issue.3 , pp. 403-414
    • Salmena, L.1    Carracedo, A.2    Pandolfi, P.P.3
  • 14
    • 51849111556 scopus 로고    scopus 로고
    • PI3K pathway alterations in cancer: Variations on a theme
    • Yuan, T. L. and Cantley, L. C. (2008) PI3K pathway alterations in cancer: Variations on a theme Oncogene 27, 5497-5510
    • (2008) Oncogene , vol.27 , pp. 5497-5510
    • Yuan, T.L.1    Cantley, L.C.2
  • 16
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-Kinase: Implications for development, immunity, homeostasis, and cancer
    • DOI 10.1146/annurev.cellbio.17.1.615
    • Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J., and Waterfield, M. D. (2001) Cellular function of phosphoinositide 3-kinases: Implications for development, immunity, homeostasis, and cancer Annu. Rev. Cell Dev. Biol. 17, 615-675 (Pubitemid 33096187)
    • (2001) Annual Review of Cell and Developmental Biology , vol.17 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3    White, S.4    Timms, J.5    Waterfield, M.D.6
  • 17
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • DOI 10.1074/jbc.273.22.13375
    • Maehama, T. and Dixon, J. E. (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate J. Biol. Chem. 273, 13375-13378 (Pubitemid 28268370)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 19
    • 33745888913 scopus 로고    scopus 로고
    • PTEN function in normal and neoplastic growth
    • DOI 10.1016/j.canlet.2005.11.042, PII S0304383505010219
    • Chow, L. M. L. and Baker, S. J. (2006) PTEN function in normal and neoplastic growth Cancer Lett. 241, 184-196 (Pubitemid 44163047)
    • (2006) Cancer Letters , vol.241 , Issue.2 , pp. 184-196
    • Chow, L.M.L.1    Baker, S.J.2
  • 29
    • 0034194786 scopus 로고    scopus 로고
    • Biotinylated phosphatidylinositol 3,4,5-trisphosphate as affinity ligand
    • DOI 10.1006/abio.2000.4525
    • Wang, D. S., Ching, T. T., St Pyrek, J., and Chen, C. S. (2000) Biotinylated phosphatidylinositol 3,4,5-trisphosphate as affinity ligand Anal. Biochem. 280, 301-307 (Pubitemid 30308086)
    • (2000) Analytical Biochemistry , vol.280 , Issue.2 , pp. 301-307
    • Wang, D.-S.1    Ching, T.-T.2    St. Pyrek, J.3    Chen, C.-S.4
  • 32
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry
    • Cravatt, B. F., Wright, A. T., and Kozarich, J. W. (2008) Activity-based protein profiling: From enzyme chemistry Annu. Rev. Biochem. 77, 383-414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 34
    • 77956516299 scopus 로고    scopus 로고
    • Proteome-wide detection of phospholipid-protein interactions in mitochondria by photocrosslinking and click chemistry
    • Gubbens, J. and de Kroon, A. (2010) Proteome-wide detection of phospholipid-protein interactions in mitochondria by photocrosslinking and click chemistry Mol. BioSyst. 6, 1751-1759
    • (2010) Mol. BioSyst. , vol.6 , pp. 1751-1759
    • Gubbens, J.1    De Kroon, A.2
  • 35
    • 77950511344 scopus 로고    scopus 로고
    • Activity-based probes that target functional subclasses of phospholipases in proteomes
    • Tully, S. E. and Cravatt, B. F. (2010) Activity-based probes that target functional subclasses of phospholipases in proteomes J. Am. Chem. Soc. 132, 3264-3265
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3264-3265
    • Tully, S.E.1    Cravatt, B.F.2
  • 36
    • 68349110882 scopus 로고    scopus 로고
    • Synthesis of modular headgroup conjugates corresponding to all seven phosphatidylinositol polyphosphate isomers for convenient probe generation
    • Gong, D., Bostic, H. E., Smith, M. D., and Best, M. D. (2009) Synthesis of modular headgroup conjugates corresponding to all seven phosphatidylinositol polyphosphate isomers for convenient probe generation Eur. J. Org. Chem., 4170-4179
    • (2009) Eur. J. Org. Chem. , pp. 4170-4179
    • Gong, D.1    Bostic, H.E.2    Smith, M.D.3    Best, M.D.4
  • 37
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • DOI 10.1016/j.chembiol.2004.03.012, PII S1074552104000961
    • Speers, A. E. and Cravatt, B. F. (2004) Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 11, 535-546 (Pubitemid 38511759)
    • (2004) Chemistry and Biology , vol.11 , Issue.4 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 38
    • 72449154666 scopus 로고    scopus 로고
    • Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation
    • Hong, V., Presolski, S. I., Ma, C., and Finn, M. G. (2009) Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation Angew. Chem., Int. Ed. 48, 9879-9883
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 9879-9883
    • Hong, V.1    Presolski, S.I.2    Ma, C.3    Finn, M.G.4
  • 39
    • 36148957855 scopus 로고    scopus 로고
    • Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains
    • DOI 10.1074/jbc.M703517200
    • Manna, D., Albanese, A., Park, W. S., and Cho, W. (2007) Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains J. Biol. Chem. 282, 32093-32105 (Pubitemid 350106465)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 32093-32105
    • Manna, D.1    Albanese, A.2    Wei, S.P.3    Cho, W.4
  • 40
    • 52249114702 scopus 로고    scopus 로고
    • Synthesis and convenient functionalization of azide-labeled diacylglycerol analogues for modular access to biologically active lipid probes
    • Smith, M. D., Gong, D. H., Sudhahar, C. G., Reno, J. C., Stahelin, R. V., and Best, M. D. (2008) Synthesis and convenient functionalization of azide-labeled diacylglycerol analogues for modular access to biologically active lipid probes Bioconjugate Chem. 19, 1855-1863
    • (2008) Bioconjugate Chem. , vol.19 , pp. 1855-1863
    • Smith, M.D.1    Gong, D.H.2    Sudhahar, C.G.3    Reno, J.C.4    Stahelin, R.V.5    Best, M.D.6
  • 42
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • DOI 10.1021/ja034490h
    • Speers, A. E., Adam, G. C., and Cravatt, B. F. (2003) Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition J. Am. Chem. Soc. 125, 4686-4687 (Pubitemid 36505343)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.16 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 44
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • DOI 10.1021/pr025556v
    • Peng, J. M., Elias, J. E., Thoreen, C. C., Licklider, L. J., and Gygi, S. P. (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome J. Proteome Res. 2, 43-50 (Pubitemid 36207189)
    • (2003) Journal of Proteome Research , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 45
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P., Wolters, D., and Yates, J. R. (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 19, 242-247 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 46
    • 0033951038 scopus 로고    scopus 로고
    • Using photolabile ligands in drug discovery and development
    • DOI 10.1016/S0167-7799(99)01402-X, PII S016777999901402X
    • Dorman, G. and Prestwich, G. D. (2000) Using photolabile ligands in drug discovery and development Trends Biotechnol. 18, 64-77 (Pubitemid 30084698)
    • (2000) Trends in Biotechnology , vol.18 , Issue.2 , pp. 64-77
    • Dorman, G.1    Prestwich, G.D.2
  • 47
    • 21144455523 scopus 로고    scopus 로고
    • A new chemical probe for proteomics of carbohydrate-binding proteins
    • DOI 10.1002/cbic.200400209
    • Ballell, L., Alink, K. J., Slijper, M., Versluis, C., Liskamp, R. M. J., and Pieters, R. J. (2005) A new chemical probe for proteomics of carbohydrate-binding proteins ChemBioChem 6, 291-295 (Pubitemid 40879741)
    • (2005) ChemBioChem , vol.6 , Issue.2 , pp. 291-295
    • Ballell, L.1    Alink, K.J.2    Slijper, M.3    Versluis, C.4    Liskamp, R.M.J.5    Pieters, R.J.6
  • 50
    • 80053015717 scopus 로고    scopus 로고
    • Exploiting bioorthogonal chemistry to elucidate protein-lipid binding interactions and other biological roles of phospholipids
    • Best, M. D., Rowland, M. M., and Bostic, H. E. Exploiting bioorthogonal chemistry to elucidate protein-lipid binding interactions and other biological roles of phospholipids Acc. Chem. Res. 44, 686-698
    • Acc. Chem. Res. , vol.44 , pp. 686-698
    • Best, M.D.1    Rowland, M.M.2    Bostic, H.E.3
  • 51
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E. M. and Bertozzi, C. R. (2009) Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality Angew. Chem., Int. Ed. 48, 6974-6998
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 52
    • 67650474557 scopus 로고    scopus 로고
    • Click chemistry and bioorthogonal reactions: Unprecedented selectivity in the labeling of biological molecules
    • Best, M. D. (2009) Click chemistry and bioorthogonal reactions: Unprecedented selectivity in the labeling of biological molecules Biochemistry 48, 6571-6584
    • (2009) Biochemistry , vol.48 , pp. 6571-6584
    • Best, M.D.1
  • 53
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • DOI 10.1016/0092-8674(95)90219-8
    • Ferguson, K. M., Lemmon, M. A., Schlessinger, J., and Sigler, P. B. (1995) Structure of the high-affinity complex of inositol trisphosphate with a phospholipase-C pleckstrin homology domain Cell 83, 1037-1046 (Pubitemid 26006545)
    • (1995) Cell , vol.83 , Issue.6 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 57
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M. A., Ferguson, K. M., Obrien, R., Sigler, P. B., and Schlessinger, J. (1995) Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain Proc. Natl. Acad. Sci. U.S.A. 92, 10472-10476
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    Obrien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 58
    • 0001484549 scopus 로고    scopus 로고
    • Touching All the Bases: Synthesis of Inositol Polyphosphate and Phosphoinositide Affinity Probes from Glucose
    • Prestwich, G. D. (1996) Touching all the bases: Synthesis of inositol polyphosphate and phosphoinositide affinity probes from glucose Acc. Chem. Res. 29, 503-513 (Pubitemid 126454581)
    • (1996) Accounts of Chemical Research , vol.29 , Issue.10 , pp. 503-513
    • Prestwich, G.D.1
  • 59
    • 0029857093 scopus 로고    scopus 로고
    • 3
    • DOI 10.1021/jo961226g
    • Gu, Q. M. and Prestwich, G. D. (1996) Synthesis of phosphotriester analogues of the phosphoinositides PtdIns(4,5)P-2 and PtdIns(3,4,5)P-3 J. Org. Chem. 61, 8642-8647 (Pubitemid 26419373)
    • (1996) Journal of Organic Chemistry , vol.61 , Issue.24 , pp. 8642-8647
    • Gu, Q.-M.1    Prestwich, G.D.2
  • 61
    • 0037423253 scopus 로고    scopus 로고
    • Comprehensive and uniform synthesis of all naturally occurring phosphorylated phosphatidylinositols
    • DOI 10.1021/jo0206418
    • Kubiak, R. J. and Bruzik, K. S. (2003) Comprehensive and uniform synthesis of all naturally occurring phosphorylated phosphatidylinositols J. Org. Chem. 68, 960-968 (Pubitemid 36176620)
    • (2003) Journal of Organic Chemistry , vol.68 , Issue.3 , pp. 960-968
    • Kubiak, R.J.1    Bruzik, K.S.2
  • 62
    • 0023885218 scopus 로고
    • Semisynthetic derivatives of inositol 1,4,5-trisphosphate substituted at the 1-phosphate group: Effects on calium release from permeabilized guinea-pig parotid acinar cells and comparison with binding to alolase-A
    • Henne, V., Mayr, G. W., Grabowski, B., Koppitz, B., and Soling, H. D. (1988) Semisynthetic derivatives of inositol 1,4,5-trisphosphate substituted at the 1-phosphate group: Effects on calium release from permeabilized guinea-pig parotid acinar cells and comparison with binding to alolase-A Eur. J. Biochem. 174, 95-101
    • (1988) Eur. J. Biochem. , vol.174 , pp. 95-101
    • Henne, V.1    Mayr, G.W.2    Grabowski, B.3    Koppitz, B.4    Soling, H.D.5
  • 63
    • 0028879702 scopus 로고
    • Synthesis of d -myo-P-1-(O-aminopropyl)-inositol-1,4,5-trisphosphate affinity probes from α- D -glucose
    • Dorman, G., Chen, J., and Prestwich, G. D. (1995) Synthesis of d -myo-P-1-(O-aminopropyl)-inositol-1,4,5-trisphosphate affinity probes from α- d -glucose Tetrahedron Lett. 36, 8719-8722
    • (1995) Tetrahedron Lett. , vol.36 , pp. 8719-8722
    • Dorman, G.1    Chen, J.2    Prestwich, G.D.3
  • 64
    • 0033591669 scopus 로고    scopus 로고
    • Synthesis and evaluation of 1-position-modified inositol 1,4,5- trisphosphate analogs
    • DOI 10.1016/S0960-894X(99)00256-5, PII S0960894X99002565
    • Inoue, T., Kikuchi, K., Hirose, K., Iino, M., and Nagano, T. (1999) Synthesis and evaluation of 1-position-modified inositol 1,4,5-trisphosphate analogs Bioorg. Med. Chem. Lett. 9, 1697-1702 (Pubitemid 29278857)
    • (1999) Bioorganic and Medicinal Chemistry Letters , vol.9 , Issue.12 , pp. 1697-1702
    • Inoue, T.1    Kikuchi, K.2    Hirose, K.3    Iino, M.4    Nagano, T.5
  • 65
    • 0027116028 scopus 로고
    • New tetherable derivatives of myo- inositol 2,4,5-trisphosphates and 1,3,4-trisphosphates
    • Marecek, J. F., Estevez, V. A., and Prestwich, G. D. (1992) New tetherable derivatives of myo- inositol 2,4,5-trisphosphates and 1,3,4-trisphosphates Carbohydr. Res. 234, 65-73
    • (1992) Carbohydr. Res. , vol.234 , pp. 65-73
    • Marecek, J.F.1    Estevez, V.A.2    Prestwich, G.D.3
  • 66
    • 0037170818 scopus 로고    scopus 로고
    • Hydrophobic modifications at 1-phosphate of inositol 1,4,5-trisphosphate analogues enhance receptor binding
    • DOI 10.1016/S0960-894X(02)00044-6, PII S0960894X02000446
    • Nakanishi, W., Kikuchi, K., Inoue, T., Hirose, K., Iino, M., and Nagano, T. (2002) Hydrophobic modifications at 1-phosphate of inositol 1,4,5-trisphosphate analogues enhance receptor binding Bioorg. Med. Chem. Lett. 12, 911-913 (Pubitemid 34214973)
    • (2002) Bioorganic and Medicinal Chemistry Letters , vol.12 , Issue.6 , pp. 911-913
    • Nakanishi, W.1    Kikuchi, K.2    Inoue, T.3    Hirose, K.4    Iino, M.5    Nagano, T.6
  • 68
    • 0001012024 scopus 로고
    • Tethered IP3: Synthesis and biochemical applications of the 1- O -(3-aminopropyl) ester of inositol 1,4,5-trisphosphate
    • Prestwich, G. D., Marecek, J. F., Mourey, R. J., Theibert, A. B., Ferris, C. D., Danoff, S. K., and Snyder, S. H. (1991) Tethered IP3: Synthesis and biochemical applications of the 1- O -(3-aminopropyl) ester of inositol 1,4,5-trisphosphate J. Am. Chem. Soc. 113, 1822-1825
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1822-1825
    • Prestwich, G.D.1    Marecek, J.F.2    Mourey, R.J.3    Theibert, A.B.4    Ferris, C.D.5    Danoff, S.K.6    Snyder, S.H.7
  • 69
    • 0025647105 scopus 로고
    • Synthesis and application of photoaffinity analogs of inositol 1,4,5-trisphosphate selectively substituted at the 1-phosphate group
    • Schafer, R., Nehlssahabandu, M., Grabowsky, B., Dehlingerkremer, M., Schulz, I., and Mayr, G. W. (1990) Synthesis and application of photoaffinity analogs of inositol 1,4,5-trisphosphate selectively substituted at the 1-phosphate group Biochem. J. 272, 817-825
    • (1990) Biochem. J. , vol.272 , pp. 817-825
    • Schafer, R.1    Nehlssahabandu, M.2    Grabowsky, B.3    Dehlingerkremer, M.4    Schulz, I.5    Mayr, G.W.6
  • 70
    • 0027111584 scopus 로고
    • Syntheses of d - Myo -inositol 1,4,5-trisphosphate affinity ligands
    • Tegge, W. and Ballou, C. E. (1992) Syntheses of d-myo -inositol 1,4,5-trisphosphate affinity ligands Carbohydr. Res. 230, 63-77
    • (1992) Carbohydr. Res. , vol.230 , pp. 63-77
    • Tegge, W.1    Ballou, C.E.2
  • 71
    • 68949116076 scopus 로고    scopus 로고
    • Modular synthesis of biologically active phosphatidic acid probes using click chemistry
    • Smith, M. D., Sudhahar, C. G., Gong, D., Stahelin, R. V., and Best, M. D. (2009) Modular synthesis of biologically active phosphatidic acid probes using click chemistry Mol. BioSyst. 5, 962-972
    • (2009) Mol. BioSyst. , vol.5 , pp. 962-972
    • Smith, M.D.1    Sudhahar, C.G.2    Gong, D.3    Stahelin, R.V.4    Best, M.D.5
  • 72
    • 0030991386 scopus 로고    scopus 로고
    • High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity
    • DOI 10.1074/jbc.272.13.8474
    • Frech, M., Andjelkovic, M., Ingley, E., Reddy, K. K., Falck, J. R., and Hemmings, B. A. (1997) High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC protein kinase B and their influence on kinase activity J. Biol. Chem. 272, 8474-8481 (Pubitemid 27147810)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.13 , pp. 8474-8481
    • Frech, M.1    Andjelkovic, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 73
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James, S. R., Downes, C. P., Gigg, R., Grove, S. J. A., Holmes, A. B., and Alessi, D. R. (1996) Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation Biochem. J. 315, 709-713 (Pubitemid 26147592)
    • (1996) Biochemical Journal , vol.315 , Issue.3 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.A.4    Holmes, A.B.5    Alessi, D.R.6
  • 76
    • 4444324951 scopus 로고    scopus 로고
    • Polytriazoles as copper(I)-stabilizing ligands in catalysis
    • DOI 10.1021/ol0493094
    • Chan, T. R., Hilgraf, R., Sharpless, K. B., and Fokin, V. V. (2004) Polytriazoles as copper(I)-stabilizing ligands in catalysis Org. Lett. 6, 2853-2855 (Pubitemid 39178025)
    • (2004) Organic Letters , vol.6 , Issue.17 , pp. 2853-2855
    • Chan, T.R.1    Hilgraf, R.2    Sharpless, K.B.3    Fokin, V.V.4
  • 77
    • 0029644596 scopus 로고
    • Method to correlate tandem mass-spectra of modified peptides to amino-acid sequences in the protein database
    • Yates, J. R., III, Eng, J. K., McCormack, A. L., and Schieltz, D. (1995) Method to correlate tandem mass-spectra of modified peptides to amino-acid sequences in the protein database Anal. Chem. 67, 1426-1436
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 78
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., and Yates, J. R. (2002) DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics J. Proteome Res. 1, 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3
  • 79
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • DOI 10.1021/ac050846r
    • Zybailov, B., Coleman, M. K., Florens, L., and Washburn, M. P. (2005) Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling Anal. Chem. 77, 6218-6224 (Pubitemid 41436955)
    • (2005) Analytical Chemistry , vol.77 , Issue.19 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4
  • 80
    • 38649098761 scopus 로고    scopus 로고
    • Characterization of global yeast quantitative proteome data generated from the wild-type and glucose repression Saccharomyces cerevisiae strains: The comparison of two quantitative methods
    • DOI 10.1021/pr700580m
    • Usaite, R., Wohlschlegel, J., Venable, J. D., Park, S. K., Nielsen, J., Olsson, L., and Yates, J. R. (2008) Characterization of global yeast quantitative proteome data generated from the wild-type and glucose repression Saccharomyces cerevisiae strains: The comparison of two quantitative methods J. Proteome Res. 7, 266-275 (Pubitemid 351171139)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 266-275
    • Usaite, R.1    Wohlschlegel, J.2    Venable, J.D.3    Park, S.K.4    Nielsen, J.5    Olsson, L.6    Yates III, J.R.7
  • 81
    • 33749671593 scopus 로고    scopus 로고
    • An Enzyme that Regulates Ether Lipid Signaling Pathways in Cancer Annotated by Multidimensional Profiling
    • DOI 10.1016/j.chembiol.2006.08.008, PII S1074552106003000
    • Chiang, K. P., Niessen, S., Saghatelian, A., and Cravatt, B. F. (2006) An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling Chem. Biol. 13, 1041-1050 (Pubitemid 44557068)
    • (2006) Chemistry and Biology , vol.13 , Issue.10 , pp. 1041-1050
    • Chiang, K.P.1    Niessen, S.2    Saghatelian, A.3    Cravatt, B.F.4
  • 82
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness
    • Jessani, N., Liu, Y. S., Humphrey, M., and Cravatt, B. F. (2002) Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness Proc. Natl. Acad. Sci. U.S.A. 99, 10335-10340
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10335-10340
    • Jessani, N.1    Liu, Y.S.2    Humphrey, M.3    Cravatt, B.F.4
  • 83
    • 43749107913 scopus 로고    scopus 로고
    • Application of activity-based probes to the study of enzymes involved in cancer progression
    • DOI 10.1016/j.gde.2007.12.001, PII S0959437X07002134
    • Paulick, M. G. and Bogyo, M. (2008) Application of activity-based probes to the study of enzymes involved in cancer progression Curr. Opin. Genet. Dev. 18, 97-106 (Pubitemid 351694441)
    • (2008) Current Opinion in Genetics and Development , vol.18 , Issue.1 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 84
  • 86
    • 8844268481 scopus 로고    scopus 로고
    • Discovering disease-associated enzymes by proteome reactivity profiling
    • DOI 10.1016/j.chembiol.2004.08.023, PII S1074552104002686
    • Barglow, K. T. and Cravatt, B. F. (2004) Discovering disease-associated enzymes by proteome reactivity profiling Chem. Biol. 11, 1523-1531 (Pubitemid 39527279)
    • (2004) Chemistry and Biology , vol.11 , Issue.11 , pp. 1523-1531
    • Barglow, K.T.1    Cravatt, B.F.2
  • 87
    • 22744443710 scopus 로고    scopus 로고
    • Inositide evolution - Towards turtle domination?
    • DOI 10.1113/jphysiol.2005.087387
    • Irvine, R. F. (2005) Inositide evolution: Towards turtle domination? J. Physiol. 566, 295-300 (Pubitemid 41030540)
    • (2005) Journal of Physiology , vol.566 , Issue.2 , pp. 295-300
    • Irvine, R.F.1
  • 88
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • DOI 10.1038/35073015
    • Irvine, R. F. and Schell, M. J. (2001) Back in the water: The return of the inositol phosphates Nat. Rev. Mol. Cell Biol. 2, 327-338 (Pubitemid 33674045)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 89
    • 0034113153 scopus 로고    scopus 로고
    • Novel functional PI 3-kinase antagonists inhibit cell growth and tumorigenicity in human cancer cell lines
    • Razzini, G., Berrie, C. P., Vignati, S., Broggini, M., Mascetta, G., Brancaccio, A., and Falasca, M. (2000) Novel functional PI 3-kinase antagonists inhibit cell growth and tumorigenicity in human cancer cell lines FASEB J. 14, 1179-1187 (Pubitemid 30350400)
    • (2000) FASEB Journal , vol.14 , Issue.9 , pp. 1179-1187
    • Razzini, G.1    Berrie, C.P.2    Vignati, S.3    Broggini, M.4    Mascetta, G.5    Brancaccio, A.6    Falasca, M.7
  • 91
    • 0000949572 scopus 로고    scopus 로고
    • A Conformationally Restricted Cyclic Phosphate Analogue of Inositol Trisphosphate: Synthesis and Physicochemical Properties
    • Riley, A. M., Guedat, P., Schlewer, G., Spiess, B., and Potter, B. V. L. (1998) A conformationally restricted cyclic phosphate analogue of inositol trisphosphate: Synthesis and physicochemical properties J. Org. Chem. 63, 295-305 (Pubitemid 128494073)
    • (1998) Journal of Organic Chemistry , vol.63 , Issue.2 , pp. 295-305
    • Riley, A.M.1    Guedat, P.2    Schlewer, G.3    Spiess, B.4    Potter, B.V.L.5


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