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Volumn 4, Issue 9, 2009, Pages 733-739

High affinity binding to profilin by a covalently constrained, soluble mimic of phosphatidylinositol-4,5-bisphosphate micelles

Author keywords

[No Author keywords available]

Indexed keywords

DENDRIMER; DIACYLGLYCEROL; INOSITOL 1,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PROFILIN;

EID: 70349278458     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb900121r     Document Type: Article
Times cited : (5)

References (72)
  • 1
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • DOI 10.1038/nrc1819, PII N1819
    • Cully, M., You, H., Levine, A. J., and Mak, T. W. (2006) Beyond PTEN mutations: the PI3K pathways as an integrator of multiple inputs during tumorigenesis, Nat. Rev. Cancer 6, 184-192. (Pubitemid 43292562)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 2
    • 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
  • 3
    • 0035478249 scopus 로고    scopus 로고
    • Structural properties of lipid-binding sites in cytoskeletal proteins
    • DOI 10.1016/S0968-0004(01)01927-2, PII S0968000401019272
    • Niggli, V. (2001) Structural properties of lipidbinding sites in cytoskeletal proteins, Trends Biochem. Sci. 26, 604-611. (Pubitemid 32926756)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 604-611
    • Niggli, V.1
  • 4
  • 5
    • 2942718545 scopus 로고    scopus 로고
    • PI-loting membrane traffic
    • De Matteis, M. A., and Godi, A. (2004) PI-loting membrane traffic, Nat. Cell Biol. 6, 487-492.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 487-492
    • De Matteis, M.A.1    Godi, A.2
  • 6
    • 28844478464 scopus 로고    scopus 로고
    • Phosphoinositide regulation of clathrin-mediated endocytosis
    • Haucke, V. (2005) Phosphoinositide regulation of clathrin-mediated endocytosis, Biochem. Soc. Trans. 33, 1285-1289.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1285-1289
    • Haucke, V.1
  • 7
    • 21044443928 scopus 로고    scopus 로고
    • Inositol-lipid binding motifs: Signal integrators through protein-lipid and protein-protein interactions
    • Balla, T. (2005) Inositol-lipid binding motifs: signal integrators through protein - lipid and protein - protein interactions, J. Cell Sci. 118, 2093-2104.
    • (2005) J. Cell Sci. , vol.118 , pp. 2093-2104
    • Balla, T.1
  • 8
    • 33748462297 scopus 로고    scopus 로고
    • Membrane binding domains
    • Hurley, J. H. (2006) Membrane binding domains, Biochem. Biophys. Acta 1761, 805-811.
    • (2006) Biochem. Biophys. Acta , vol.1761 , pp. 805-811
    • Hurley, J.H.1
  • 9
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon, M. A. (2003) Phosphoinositide recognition domains, Traffic 4, 201-213.
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 10
    • 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) Membraneprotein interactions in cell signaling and membrane trafficking, Annu. Rev. Biophys. Biomol. Struct. 34, 119-151112 plates. (Pubitemid 40847721)
    • (2005) Annual Review of Biophysics and Biomolecular Structure , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 11
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008) Membrane recognition by phospholipid-binding domains, Nat. Rev. Mol. Cell Biol. 9, 99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 12
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • DOI 10.1038/314472a0
    • Lassing, I., and Lindberg, U. (1985) Specific interaction between phsophatidylinositol 4,5-bisphosphate and profilactin, Nature 314, 835-838. (Pubitemid 15145594)
    • (1985) Nature , vol.314 , Issue.6010 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 14
    • 0035969971 scopus 로고    scopus 로고
    • Full-contact domain labeling: Identification of a novel phosphoinositide binding site on gelsolin that requires the complete protein
    • DOI 10.1021/bi000996q
    • Feng, L., Mejillano, M., Yin, H. L., Chen, J., and Prestwich, G. D. (2001) Full-contact domain labeling: Identification of a novel phosphoinositide binding site on gelsolin that requires the complete protein, Biochemistry 40, 904-913. (Pubitemid 32108582)
    • (2001) Biochemistry , vol.40 , Issue.4 , pp. 904-913
    • Feng, L.1    Mejillano, M.2    Yin, H.L.3    Chen, J.4    Prestwich, G.D.5
  • 15
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequesteration of phosphatidylinositol 4,5- bisphospate by the basic effector domain of myristolated alanine-rich C kinase substrate is due to nonspecific electrostatic interaction
    • Wang, J., Gambhir, A., Hangyas-Mihalyne, G., Murray, D., Golbebiewska, U., and McLaughlin, S. (2002) Lateral sequesteration of phosphatidylinositol 4,5- bisphospate by the basic effector domain of myristolated alanine-rich C kinase substrate is due to nonspecific electrostatic interaction, J. Biol. Chem. 277, 34401-34412.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    Hangyas-Mihalyne, G.3    Murray, D.4    Golbebiewska, U.5    McLaughlin, S.6
  • 16
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide binding sequence in an actin monomer-binding domain of gelsolin
    • Yu, F. X., Sun, H. Q., Janmey, P., and Yin, H. L. (1992) Identification of a polyphosphoinositide binding sequence in an actin monomer-binding domain of gelsolin, J. Biol. Chem. 267, 14616-14621.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmey, P.3    Yin, H.L.4
  • 17
    • 41849146759 scopus 로고    scopus 로고
    • Hydrogen bonding and binding of polybasic residues with negatively charged mixed lipid monolayers
    • Lorenz, C. D., Faraudo, J., and Travesset, A. (2008) Hydrogen bonding and binding of polybasic residues with negatively charged mixed lipid monolayers, Langmuir 24, 1654-1658.
    • (2008) Langmuir , vol.24 , pp. 1654-1658
    • Lorenz, C.D.1    Faraudo, J.2    Travesset, A.3
  • 18
    • 25844454807 scopus 로고    scopus 로고
    • Coincidence detection in phosphoinositide signaling
    • Carlton, J. G., and Cullen, P. J. (2005) Coincidence detection in phosphoinositide signaling, Trends Cell Biol. 15, 540-547.
    • (2005) Trends Cell Biol. , vol.15 , pp. 540-547
    • Carlton, J.G.1    Cullen, P.J.2
  • 19
    • 0034722326 scopus 로고    scopus 로고
    • 2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution
    • 2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution, J. Cell Biol. 151, 1067-1080.
    • (2000) J. Cell Biol. , vol.151 , pp. 1067-1080
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 20
    • 0038159324 scopus 로고    scopus 로고
    • Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate
    • DOI 10.1242/jcs.00448
    • Bompard, G., Martin, M., Roy, C., Vignon, F., and Freiss, G. (2003) Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate, J. Cell Sci. 116, 2519-2530. (Pubitemid 36790133)
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2519-2530
    • Bompard, G.1    Martin, M.2    Roy, C.3    Vignon, F.4    Freiss, G.5
  • 22
    • 0033766768 scopus 로고    scopus 로고
    • Myosin-X, a novel myosin with pleckstrin homolgy domains, associates with regions of dynamic actin
    • Berg, J. S., Derfler, B. H., Pennisi, C. M., Corey, D. P., and Cheney, R. E. (2000) Myosin-X, a novel myosin with pleckstrin homolgy domains, associates with regions of dynamic actin, J. Cell Sci. 113, 3439-3451.
    • (2000) J. Cell Sci. , vol.113 , pp. 3439-3451
    • Berg, J.S.1    Derfler, B.H.2    Pennisi, C.M.3    Corey, D.P.4    Cheney, R.E.5
  • 23
    • 0032538636 scopus 로고    scopus 로고
    • The pleckstrin homology domains of dynamin isoforms require oligomerization for high affinity phosphoinositide binding
    • DOI 10.1074/jbc.273.42.27725
    • Klein, D. E., Lee, A., Frank, D. W., Marks, M. S., and Lemmon, M. A. (1998) The pleckstrin homology domains of dynamin isoforms require oligomerization for high affinity phosphoinositide binding, J. Biol. Chem. 273, 27725-27733. (Pubitemid 28500499)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27725-27733
    • Klein, D.E.1    Lee, A.2    Frank, D.W.3    Marks, M.S.4    Lemmon, M.A.5
  • 24
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M., Seok-Ki, C., and Whitesides, G. M. (1998) Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors, Angew. Chem., Int. Ed. 37, 2754-2794. (Pubitemid 29008561)
    • (1998) Angewandte Chemie - International Edition , vol.37 , Issue.20 , pp. 2754-2794
    • Mammen, M.1    Choi, S.-K.2    Whitesides, G.M.3
  • 25
    • 33746296180 scopus 로고    scopus 로고
    • Synthetic multivalent ligands as probes of signal transduction
    • Kiessling, L. L., Gestwicki, J. E., and Strong, L. E. (2006) Synthetic multivalent ligands as probes of signal transduction, Angew. Chem., Int. Ed. 45, 2348-2368.
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 2348-2368
    • Kiessling, L.L.1    Gestwicki, J.E.2    Strong, L.E.3
  • 26
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycosidic effect
    • Lundquist, J. J., and Toone, E. J. (2002) The cluster glycosidic effect, Chem. Rev. 102, 555-578.
    • (2002) Chem. Rev. , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 28
    • 62149093965 scopus 로고    scopus 로고
    • Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins
    • Bae, Y. H., Ding, Z., Zou, L., Wells, A., Gertler, F., and Roy, P. (2009) Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins, J. Cell. Physiol. 219, 354-364.
    • (2009) J. Cell. Physiol. , vol.219 , pp. 354-364
    • Bae, Y.H.1    Ding, Z.2    Zou, L.3    Wells, A.4    Gertler, F.5    Roy, P.6
  • 29
    • 58149269841 scopus 로고    scopus 로고
    • Profilin-1 overexpression upregulates PTEN and suppresses AKT activation in breast cancer cells
    • Das, T., Bae, Y. H., Wells, A., and Roy, P. (2008) Profilin-1 overexpression upregulates PTEN and suppresses AKT activation in breast cancer cells, J. Cell. Physiol. 218, 436-443.
    • (2008) J. Cell. Physiol. , vol.218 , pp. 436-443
    • Das, T.1    Bae, Y.H.2    Wells, A.3    Roy, P.4
  • 30
    • 4143120075 scopus 로고    scopus 로고
    • The role of profilin complexes in cell motility and other cellular processes
    • Witke, W. (2004) The role of profilin complexes in cell motility and other cellular processes, Trends Cell Biol. 14, 461-469.
    • (2004) Trends Cell Biol. , vol.14 , pp. 461-469
    • Witke, W.1
  • 32
    • 0029946425 scopus 로고    scopus 로고
    • Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity
    • Lu, P. J., Shieh, W. R., Rhee, S. G., Yin, H. L., and Chen, C. S. (1996) Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity, Biochemistry 35, 14027-14033.
    • (1996) Biochemistry , vol.35 , pp. 14027-14033
    • Lu, P.J.1    Shieh, W.R.2    Rhee, S.G.3    Yin, H.L.4    Chen, C.S.5
  • 33
    • 0025517560 scopus 로고
    • The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C
    • Machesky, L. M., Goldschmidt-Clermont, P. J., and Pollard, T. D. (1990) The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C, Cell Reg. 1, 937-950.
    • (1990) Cell Reg. , vol.1 , pp. 937-950
    • Machesky, L.M.1    Goldschmidt-Clermont, P.J.2    Pollard, T.D.3
  • 36
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin
    • Sohn, R. H., Chen, J., Koblan, K. S., Bray, P. F., and Goldschmidt-Clermont, P. J. (1995) Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin, J. Biol. Chem. 270, 21114-21120.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 37
    • 0025760751 scopus 로고
    • Regulation of phospholipase C-γ1 by profilin and tyrosine phosphorylation
    • Goldschmidt-Clermont, P. J., Kim, J. W., Machesky, L. M., Rhee, S. G., and Pollard, T. D. (1991) Regulation of phospholipase C-γ1 by profilin and tyrosine phosphorylation, Science 251, 1231-1233. (Pubitemid 21926219)
    • (1991) Science , vol.251 , Issue.4998 , pp. 1231-1233
    • Goldschmidt-Clermont, P.J.1    Kim, J.W.2    Machesky, L.M.3    Rhee, S.G.4    Pollard, T.D.5
  • 38
    • 0025373701 scopus 로고
    • Starburst dendrimers: Molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter
    • Tomalia, D. A., Naylor, A. M., and Goddard Iii, W. A. (1990) Starburst dendrimers: molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter, Angew. Chem., Int. Ed. Engl. 29, 138-175.
    • (1990) Angew. Chem., Int. Ed. Engl. , vol.29 , pp. 138-175
    • Tomalia, D.A.1    Naylor, A.M.2    Goddard III, W.A.3
  • 40
    • 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.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 503-513
    • Prestwich, G.D.1
  • 42
    • 0027116051 scopus 로고
    • An efficient chemoenzymic access to optically active myoinositol polyphophates
    • Gou, D. M., Liu, Y. C., and Chen, C. S. (1992) An efficient chemoenzymic access to optically active myoinositol polyphophates, Carbohydr. Res. 234, 51-64.
    • (1992) Carbohydr. Res. , vol.234 , pp. 51-64
    • Gou, D.M.1    Liu, Y.C.2    Chen, C.S.3
  • 43
    • 34347344067 scopus 로고    scopus 로고
    • Synthesis and characterization of covalent mimics of phosphatidylinositol-4,5-bisphosphate micelles
    • DOI 10.1021/bm061166g
    • Webb, S. A., Stewart, N. K., Belcher, L. J., Mechref, Y., Tomaszewski, J. W., Wu, G., Novotny, M. V., and Oakley, M. G. (2007) Synthesis and characterization of covalent mimics of phosphatidylinositol-4,5-bisphosphate micelles, Biomacromolecules 8, 1790-1793. (Pubitemid 47009953)
    • (2007) Biomacromolecules , vol.8 , Issue.6 , pp. 1790-1793
    • Webb, S.A.1    Stewart, N.K.2    Belcher, L.J.3    Mechref, Y.4    Tomaszewski, J.W.5    Wu, G.6    Novotny, M.V.7    Oakley, M.G.8
  • 44
    • 0019469654 scopus 로고
    • Structure of molecular aggregates of 1-(3-sn-phosphatidy)-L-myo-inositol 3,4-bis(phosphate) in water
    • Sugiura, Y. (1981) Structure of molecular aggregates of 1-(3-sn-phosphatidy)-L-myo-inositol 3,4-bis(phosphate) in water, Biochim. Biophys. Acta 641, 148-159.
    • (1981) Biochim. Biophys. Acta , vol.641 , pp. 148-159
    • Sugiura, Y.1
  • 46
    • 0034834503 scopus 로고    scopus 로고
    • Mannose functionalization of a sixth generation dendrimer
    • Woller, E. K., and Cloninger, M. J. (2001) Mannose functionalization of a sixth generation dendrimer, Biomacromolecules 2, 1052-1054.
    • (2001) Biomacromolecules , vol.2 , pp. 1052-1054
    • Woller, E.K.1    Cloninger, M.J.2
  • 47
    • 0037050414 scopus 로고    scopus 로고
    • The lectin-binding properties of six generations of mannosefunctionalized dendrimers
    • Woller, E. K., and Cloninger, M. J. (2002) The lectin-binding properties of six generations of mannosefunctionalized dendrimers, Org. Lett. 4, 7-10.
    • (2002) Org. Lett. , vol.4 , pp. 7-10
    • Woller, E.K.1    Cloninger, M.J.2
  • 48
    • 33845297637 scopus 로고
    • Squaric acid diethyl ester: A new coupling reagent for the formation of drug biopolymer conjugates. Synthesis of squaric acid ester amides and diamides
    • Tietze, L. F., Arlt, M., Beller, M., Glusenkamp, K., Jahde, E., and Rajewsky, M. F. (1991) Squaric acid diethyl ester: A new coupling reagent for the formation of drug biopolymer conjugates. Synthesis of squaric acid ester amides and diamides, Chem. Ber. 124, 1215-1221.
    • (1991) Chem. Ber. , vol.124 , pp. 1215-1221
    • Tietze, L.F.1    Arlt, M.2    Beller, M.3    Glusenkamp, K.4    Jahde, E.5    Rajewsky, M.F.6
  • 49
    • 0033870050 scopus 로고    scopus 로고
    • Functional characterization of green fluorescent protein-profilin fusion proteins
    • DOI 10.1046/j.1432-1327.2000.01600.x
    • Wittenmayer, N., Rothkegel, M., Jockusch, B. M., and Schluter, K. (2000) Functional characterization of green fluorescent protein-profilin fusion proteins, Eur. J. Biochem. 267, 5256. (Pubitemid 30641322)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.16 , pp. 5247-5256
    • Wittenmayer, N.1    Rothkegel, M.2    Jockusch, B.M.3    Schluter, K.4
  • 50
    • 0342327310 scopus 로고    scopus 로고
    • Isolation and characterization of two mutants of human profilin I that do not bind poly(L-proline)
    • DOI 10.1016/S0014-5793(97)01376-8, PII S0014579397013768
    • Bjorkegren-Sjogren, C., Korenbaum, E., Nordberg, P., Lindberg, U., and Karlsson, R. (1997) Isolation and characterization of two mutants of human profilin I that do not bind poly(L-proline), FEBS Lett. 418, 258-264. (Pubitemid 27515936)
    • (1997) FEBS Letters , vol.418 , Issue.3 , pp. 258-264
    • Bjorkegren-Sjogren, C.1    Korenbaum, E.2    Nordberg, P.3    Lindberg, U.4    Karlsson, R.5
  • 52
    • 0023940928 scopus 로고
    • Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex
    • DOI 10.1002/jcb.240370302
    • Lassing, I., and Lindberg, U. (1988) Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex, J. Cell. Biochem. 37, 255-267. (Pubitemid 18161605)
    • (1988) Journal of Cellular Biochemistry , vol.37 , Issue.3 , pp. 255-267
    • Lassing, I.1    Lindberg, U.2
  • 53
    • 58149168847 scopus 로고    scopus 로고
    • NMR investigation of the binding between human profilin I and inositol 1,4,5-triphosphate, the soluble headgroup of phosphatidylinositol 4,5-bisphosphate
    • Richer, S. M., Stewart, N. K., Tomaszewski, J. W., Stone, M. J., and Oakley, M. G. (2008) NMR investigation of the binding between human profilin I and inositol 1,4,5-triphosphate, the soluble headgroup of phosphatidylinositol 4,5-bisphosphate, Biochemistry 47, 13455-13462.
    • (2008) Biochemistry , vol.47 , pp. 13455-13462
    • Richer, S.M.1    Stewart, N.K.2    Tomaszewski, J.W.3    Stone, M.J.4    Oakley, M.G.5
  • 54
    • 33847012205 scopus 로고    scopus 로고
    • Profilin binding to sub-micellar concentrations of phosphatidylinositol (4,5) bisphosphate and phosphatidylinositol (3,4,5) trisphosphate
    • Moens, P. D. J., and Bagatolli, L. A. (2007) Profilin binding to sub-micellar concentrations of phosphatidylinositol (4,5) bisphosphate and phosphatidylinositol (3,4,5) trisphosphate, Biochim. Biophys. Acta, Biomembr. 1768, 439-449.
    • (2007) Biochim. Biophys. Acta, Biomembr. , vol.1768 , pp. 439-449
    • Moens, P.D.J.1    Bagatolli, L.A.2
  • 56
    • 2642563771 scopus 로고    scopus 로고
    • Phosphoinositide signaling: From affinity probes to pharmaceutical targets
    • DOI 10.1016/j.chembiol.2004.03.025, PII S1074552104001176
    • Prestwich, G. D. (2004) Phosphoinositide signaling: From affinity probes to pharmaceutical targets, Chem. Biol. 11, 619-637. (Pubitemid 38708831)
    • (2004) Chemistry and Biology , vol.11 , Issue.5 , pp. 619-637
    • Prestwich, G.D.1
  • 57
    • 27944452697 scopus 로고    scopus 로고
    • Phosphoinositide-containing polymerized liposomes: Stable membrane-mimetic vesicles for protein-lipid binding analysis
    • DOI 10.1021/bc050197q
    • Ferguson, C. G., James, R. D., Bigman, C. S., Shepard, D. A., Abdiche, Y., Katsamba, P. S., Myszka, D. G., and Prestwich, G. D. (2005) Phosphoinositidecontaining polymerized liposomes: stable membrane-mimetic vesicles for protein-lipid binding analysis, Bioconjugate Chem. 16, 1475-1483. (Pubitemid 41681514)
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.6 , pp. 1475-1483
    • Ferguson, C.G.1    James, R.D.2    Bigman, C.S.3    Shepard, D.A.4    Abdiche, Y.5    Katsamba, P.S.6    Myszka, D.G.7    Prestwich, G.D.8
  • 58
    • 62549083819 scopus 로고    scopus 로고
    • Microplate-based characterization of protein-phosphoinositide binding interactions using a synthetic biotinylated headgroup analogue
    • Gong, D., Smith, M. D., Manna, D., Bostic, H. E., Cho, W., and Best, M. D. (2009) Microplate-based characterization of protein-phosphoinositide binding interactions using a synthetic biotinylated headgroup analogue, Bioconjugate Chem. 20, 310-316.
    • (2009) Bioconjugate Chem. , vol.20 , pp. 310-316
    • Gong, D.1    Smith, M.D.2    Manna, D.3    Bostic, H.E.4    Cho, W.5    Best, M.D.6
  • 59
    • 0029849231 scopus 로고    scopus 로고
    • Synthesis of the D-3 series of phosphatidylinositol phosphates
    • DOI 10.1021/jo960602u
    • Wang, D. S., and Chen, C. S. (1996) Synthesis of the D-3 series of phosphatidylinositol phosphates, J. Org. Chem. 61, 5905-5910. (Pubitemid 26287854)
    • (1996) Journal of Organic Chemistry , vol.61 , Issue.17 , pp. 5905-5910
    • Wang, D.-S.1    Chen, C.-S.2
  • 60
    • 0023199043 scopus 로고
    • Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin
    • Janmey, P. A., Iida, K., Yin, H. L., and Stossel, T. P. (1987) Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin, J. Biol. Chem. 262, 12228-12236. (Pubitemid 17137443)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.25 , pp. 12228-12236
    • Jammey, P.A.1    Iida, K.2    Yin, H.L.3    Stossel, T.P.4
  • 61
    • 33746288421 scopus 로고    scopus 로고
    • Determining selectivity of phosphoinositide-binding domains
    • Narayan, K., and Lemmon, M. A. (2006) Determining selectivity of phosphoinositide-binding domains, Methods (San Diego, CA, U.S.) 39, 122-133.
    • (2006) Methods (San Diego, CA, U.S.) , vol.39 , pp. 122-133
    • Narayan, K.1    Lemmon, M.A.2
  • 62
    • 0037960821 scopus 로고    scopus 로고
    • Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/ hydroxyl-functionalized dendrimers
    • Woller, E. K., Walter, E. D., Morgan, J. R., Singel, D. J., and Cloninger, M. J. (2003) Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/ hydroxyl- functionalized dendrimers, J. Am. Chem. Soc. 125, 8820-8826.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8820-8826
    • Woller, E.K.1    Walter, E.D.2    Morgan, J.R.3    Singel, D.J.4    Cloninger, M.J.5
  • 63
    • 24644500644 scopus 로고    scopus 로고
    • Mannose/glucose-functionalized dendrimers to investigate the predictable tunability of multivalent interactions
    • Wolfenden, M. L., and Cloninger, M. J. (2005) Mannose/glucose- functionalized dendrimers to investigate the predictable tunability of multivalent interactions, J. Am. Chem. Soc. 127, 12168-12169.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12168-12169
    • Wolfenden, M.L.1    Cloninger, M.J.2
  • 64
    • 33746685001 scopus 로고    scopus 로고
    • Carbohydrate-functionalized dendrimers to investigate the predictable tunability of multivalent interactions
    • Wolfenden, M. L., and Cloninger, M. J. (2006) Carbohydrate-functionalized dendrimers to investigate the predictable tunability of multivalent interactions, Bioconjugate Chem. 17, 958-966.
    • (2006) Bioconjugate Chem. , vol.17 , pp. 958-966
    • Wolfenden, M.L.1    Cloninger, M.J.2
  • 65
    • 0027968554 scopus 로고
    • Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli
    • DOI 10.1006/jmbi.1994.1522
    • Fedorov, A. A., Pollard, T. D., and Almo, S. C. (1994) Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli, J. Mol. Biol. 241, 480-482. (Pubitemid 24266059)
    • (1994) Journal of Molecular Biology , vol.241 , Issue.3 , pp. 480-482
    • Fedorov, A.A.1    Pollard, T.D.2    Almo, S.C.3
  • 66
    • 33745926546 scopus 로고    scopus 로고
    • Application of phosphoinositide-binding domains for the detection and quantification of specific phosphoinositides
    • DOI 10.1016/j.ab.2006.05.014, PII S0003269706003629
    • Furutani, M., Tsujita, K., Itoh, T., Ijuin, T., and Takenawa, T. (2006) Application of phosphoinositidebinding domains for the detection and quantification of specific phosphoinositides, Anal. Biochem. 355, 8-18. (Pubitemid 44041412)
    • (2006) Analytical Biochemistry , vol.355 , Issue.1 , pp. 8-18
    • Furutani, M.1    Tsujita, K.2    Itoh, T.3    Ijuin, T.4    Takenawa, T.5
  • 67
    • 0028318420 scopus 로고
    • Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy
    • Huff, S., Matsuka, Y. V., McGavin, M. J., and Ingham, K. C. (1994) Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy, J. Biol. Chem. 269, 15563-15570. (Pubitemid 24202143)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.22 , pp. 15563-15570
    • Huff, S.1    Matsuka, Y.V.2    McGavin, M.J.3    Ingham, K.C.4
  • 68
    • 0034282648 scopus 로고    scopus 로고
    • Characterization of binding between chemokine eotaxin and peptides derived from the chemokine receptor CCR3
    • DOI 10.1074/jbc.M003925200
    • Ye, J., Kohli, L. L., and Stone, M. J. (2000) Characterization of binding between the chemokine eotaxin and peptides derived from the chemokine receptor CCR3, J. Biol. Chem. 275, 27250-27257. (Pubitemid 30688082)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.35 , pp. 27250-27257
    • Ye, J.1    Kohli, L.L.2    Stone, M.J.3
  • 70
    • 0034607437 scopus 로고    scopus 로고
    • Physicochemical characterization of generation 5 polyamidoamine dendrimers
    • DOI 10.1002/(SICI)1097-0282(20000405)53:4<316::AID-BIP4>3.0.CO;2-J
    • Nourse, A., Millar, D. B., and Minton, A. P. (2000) Physicochemical characterization of generation 5 polyamidoamine dendrimers, Biopolymers 53, 316-328. (Pubitemid 30230022)
    • (2000) Biopolymers , vol.53 , Issue.4 , pp. 316-328
    • Nourse, A.1    Millar, D.B.2    Minton, A.P.3
  • 71
    • 0001613166 scopus 로고    scopus 로고
    • Asymmetric Total Synthesis of Phosphatidylinositol 3-Phosphate and 4-Phosphate Derivatives
    • Chen, J., Feng, L., and Prestwich, G. D. (1998) Asymmetric total synthesis of phosphatidylinositol 3-phosphate and 4-phosphate derivatives, J. Org. Chem. 63, 6511-6522. (Pubitemid 128498409)
    • (1998) Journal of Organic Chemistry , vol.63 , Issue.19 , pp. 6511-6522
    • Chen, J.1    Feng, L.2    Prestwich, G.D.3


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