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Volumn 18, Issue 1, 1996, Pages 35-46

The pleckstrin homology domain: An intriguing multifunctional protein module

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN; GUANOSINE TRIPHOSPHATASE; PHOSPHOPROTEIN; PLASMA PROTEIN; PLATELET PROTEIN P47; SPECTRIN;

EID: 0030040967     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950180109     Document Type: Article
Times cited : (256)

References (69)
  • 1
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995). Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 2
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., Ren, R. and Baltimore, D. (1995). Modular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 3
    • 0026059615 scopus 로고
    • The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity
    • Mayer, B. J., Jackson, P. K. and Baltimore, D. (1991). The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc Natl Acad. Sci. USA 88, 627-631.
    • (1991) Proc Natl Acad. Sci. USA , vol.88 , pp. 627-631
    • Mayer, B.J.1    Jackson, P.K.2    Baltimore, D.3
  • 4
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren, R., Mayer, B. J., Cicchetti, P. and Baltimore, D. (1993). Identification of a ten-amino acid proline-rich SH3 binding site. Science 259, 1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 5
    • 0023917142 scopus 로고
    • Molecular cloning of the major protein kinase C substrate of platelets
    • Tyers, M. et al. (1988). Molecular cloning of the major protein kinase C substrate of platelets. Nature 333, 470-473.
    • (1988) Nature , vol.333 , pp. 470-473
    • Tyers, M.1
  • 6
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signaling proteins
    • Mayer, B. J., Ren, R., Clark, K. L. and Baltimore, D. (1993). A putative modular domain present in diverse signaling proteins. Cell 73, 629-630.
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.L.3    Baltimore, D.4
  • 7
    • 0027276925 scopus 로고
    • Pleckstrin domain homology
    • Haslam, R. J., Koide, H. B. and Hemmings, B. A. (1993). Pleckstrin domain homology [letter]. Nature 363, 309-310
    • (1993) Nature , vol.363 , pp. 309-310
    • Haslam, R.J.1    Koide, H.B.2    Hemmings, B.A.3
  • 8
    • 0027304398 scopus 로고
    • Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function
    • Shaw, G. (1993). Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function Biochem. Biophys. Res. Commun. 195, 1145-1151.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 1145-1151
    • Shaw, G.1
  • 9
    • 0027183541 scopus 로고
    • The PH domain a common piece in the structural patchwork of signalling proteins Trends
    • Musacchio, A., Gibson, T., Rice, P., Thompson, J. and Saraste, M. (1993). The PH domain a common piece in the structural patchwork of signalling proteins Trends Biochem. Sci. 18, 343-348.
    • (1993) Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 10
    • 0027980089 scopus 로고
    • PH domains and phospholipases - A meaningful relationship?
    • Parker, P. J., Hemmings, B. A. and Gierschik, P. (1994). PH domains and phospholipases - a meaningful relationship? Trends Biochem. Sci. 19, 54-55.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 54-55
    • Parker, P.J.1    Hemmings, B.A.2    Gierschik, P.3
  • 11
    • 0027941128 scopus 로고
    • Tec homology (TH) adjacent to the PH domain
    • Vihinen, M., Nilsson, L. and Smith, C. I. E. (1994). Tec homology (TH) adjacent to the PH domain FEBS Lett. 350, 263-265.
    • (1994) FEBS Lett. , vol.350 , pp. 263-265
    • Vihinen, M.1    Nilsson, L.2    Smith, C.I.E.3
  • 12
    • 0028609692 scopus 로고
    • Pleckstrin homology (PH) domains in signal transduction
    • Ingley, E. and Hemmings, B. A. (1994). Pleckstrin homology (PH) domains in signal transduction. J. Cell. Biochem. 56, 436-443.
    • (1994) J. Cell. Biochem. , vol.56 , pp. 436-443
    • Ingley, E.1    Hemmings, B.A.2
  • 14
    • 0029157058 scopus 로고
    • Pleckstrin homology domains: A fact file
    • Saraste M. and Hyvönen M. (1995). Pleckstrin homology domains: a fact file. Curr. Opin. Struct. Biol. 5, 403-408.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 403-408
    • Saraste, M.1    Hyvönen, M.2
  • 17
  • 18
    • 0028836020 scopus 로고
    • Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy
    • Fushman, D., Cahill, S., Lemmon, M. A., Schlessinger, J. and Cowburn, D. (1995). Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proc. Natl Acad. Sci. USA 92, 816-820.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 816-820
    • Fushman, D.1    Cahill, S.2    Lemmon, M.A.3    Schlessinger, J.4    Cowburn, D.5
  • 19
    • 0029645869 scopus 로고
    • Solution structure of the pleckstrin homology domain of Drosophila β-spectrin
    • in press
    • Zhang, P., Talluri, S., Deng, H., Branton, D. and Wagner, G. (1995). Solution structure of the pleckstrin homology domain of Drosophila β-spectrin. Structure (in press).
    • (1995) Structure
    • Zhang, P.1    Talluri, S.2    Deng, H.3    Branton, D.4    Wagner, G.5
  • 20
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson, K. M., Lemmon, M. A., Schlessinger, J. and Sigler, P. B. (1994). Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 22
    • 0027305921 scopus 로고
    • Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice
    • Rawlings, D. J. et al. (1993). Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science 261, 358-61.
    • (1993) Science , vol.261 , pp. 358-361
    • Rawlings, D.J.1
  • 23
    • 0028943589 scopus 로고
    • Structural basis for pleckstrin homology domain mutations in X-linked agammaglobulinemia
    • Vihinen, M. et al. (1995). Structural basis for pleckstrin homology domain mutations in X-linked agammaglobulinemia. Biochemistry 34, 1475-1481.
    • (1995) Biochemistry , vol.34 , pp. 1475-1481
    • Vihinen, M.1
  • 24
    • 0026667730 scopus 로고
    • AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas
    • Cheng, J. Q. et al. (1992). AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas. Proc Natl Acad. Sci. USA 89, 9267-9271.
    • (1992) Proc Natl Acad. Sci. USA , vol.89 , pp. 9267-9271
    • Cheng, J.Q.1
  • 25
    • 0028343550 scopus 로고
    • The SH2 domain protein GRB-7 is co-amplified, overexpressed and in a tight complex with HER2 in breast cancer
    • Stein, D. et al. (1994). The SH2 domain protein GRB-7 is co-amplified, overexpressed and in a tight complex with HER2 in breast cancer. EMBO J. 13, 1331-1340.
    • (1994) EMBO J. , vol.13 , pp. 1331-1340
    • Stein, D.1
  • 26
    • 0028126564 scopus 로고
    • Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: A putative Rho/Rac guanine nucleotide exchange factor
    • Pasteris, N. G. M. et al. (1994). Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: A putative Rho/Rac guanine nucleotide exchange factor. Cell 79, 669-678.
    • (1994) Cell , vol.79 , pp. 669-678
    • Pasteris, N.G.M.1
  • 27
    • 0028225439 scopus 로고
    • Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins
    • Habets, G. G. M. et al. (1994). Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell 77, 537-549.
    • (1994) Cell , vol.77 , pp. 537-549
    • Habets, G.G.M.1
  • 28
    • 0028110120 scopus 로고
    • A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways
    • Horii, Y., Beeler, J. F., Sakaguchi, K., Tachibana, M. and Miki, T. (1994). A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways. EMBO J. 13, 4776-4786.
    • (1994) EMBO J. , vol.13 , pp. 4776-4786
    • Horii, Y.1    Beeler, J.F.2    Sakaguchi, K.3    Tachibana, M.4    Miki, T.5
  • 29
    • 0028948329 scopus 로고
    • Retroviral transduction and oncogenic selection of a cDNA encoding Dbs, a homolog of the Dbl guanine nucleotide exchange factor
    • Whitehead, I., Kirk, H. and Kay, R. (1995). Retroviral transduction and oncogenic selection of a cDNA encoding Dbs, a homolog of the Dbl guanine nucleotide exchange factor. Oncogene 10, 713-721.
    • (1995) Oncogene , vol.10 , pp. 713-721
    • Whitehead, I.1    Kirk, H.2    Kay, R.3
  • 30
    • 0029155976 scopus 로고
    • Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C
    • Whitehead, I., Kirk, H., Tognon, C., Trigo-Gonzalez, G. and Kay, R. (1995). Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C. J. Biol. Chem. 270, 18388-18395.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18388-18395
    • Whitehead, I.1    Kirk, H.2    Tognon, C.3    Trigo-Gonzalez, G.4    Kay, R.5
  • 31
    • 12044259376 scopus 로고
    • Membrane ruffling and signal transduction
    • Ridley, A. J. (1994). Membrane ruffling and signal transduction. BioEssays 16, 321-327.
    • (1994) BioEssays , vol.16 , pp. 321-327
    • Ridley, A.J.1
  • 32
    • 0027470177 scopus 로고
    • Structure, expression and chromosomal mapping of c-akt: Relationship to v-akt and its implications
    • Bellacosa, A. et al. (1993). Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications. Oncogene 8, 745-754.
    • (1993) Oncogene , vol.8 , pp. 745-754
    • Bellacosa, A.1
  • 33
    • 0026803164 scopus 로고
    • Role of βγ subunits of G proteins in targeting the β-adrenergic receptor kinase to membrane-bound receptors
    • Pitcher, J. A. et al. (1992). Role of βγ subunits of G proteins in targeting the β-adrenergic receptor kinase to membrane-bound receptors. Science 257, 1264-1267.
    • (1992) Science , vol.257 , pp. 1264-1267
    • Pitcher, J.A.1
  • 34
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • Ridgway, N. D., Dawson, P. A., Mo, Y. K., Brown, M. S. and Goldstein, J. L. (1992). Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. J Cell Biol. 116, 307-319.
    • (1992) J Cell Biol. , vol.116 , pp. 307-319
    • Ridgway, N.D.1    Dawson, P.A.2    Mo, Y.K.3    Brown, M.S.4    Goldstein, J.L.5
  • 36
    • 0028169455 scopus 로고
    • 2+-sensitive phospholipid-binding protein with very high affinity for protein kinase C
    • 2+-sensitive phospholipid-binding protein with very high affinity for protein kinase C. J. Biol. Chem. 269, 21043-21050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21043-21050
    • Liu, J.-P.1    Powell, K.A.2    Südhof, T.C.3    Robinson, P.J.4
  • 37
    • 0029020217 scopus 로고
    • The pleckstrin homology domain in insulin receptor substrate-1 sensitizes insulin signaling
    • Myers, M. G., Jr. et al. (1995). The pleckstrin homology domain in insulin receptor substrate-1 sensitizes insulin signaling. J. Biol. Chem. 270, 11715-11718.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11715-11718
    • Myers Jr., M.G.1
  • 38
    • 0029029892 scopus 로고
    • Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends on its pleckstrin homology region
    • Voliovitch, H., Schindler, D. G., Hadari, Y. R., Taylor, S. I., Accili, D. and Zick, V. (1995) Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends on its pleckstrin homology region. J Biol. Chem. 270, 18083-18087.
    • (1995) J Biol. Chem. , vol.270 , pp. 18083-18087
    • Voliovitch, H.1    Schindler, D.G.2    Hadari, Y.R.3    Taylor, S.I.4    Accili, D.5    Zick, V.6
  • 39
    • 0027481032 scopus 로고
    • The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase
    • Koch, W. J., Inglese, J., Stone, W. C. and Lefkowitz, R. J. (1993). The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase. J. Biol. Chem. 11, 8256-8260.
    • (1993) J. Biol. Chem. , vol.11 , pp. 8256-8260
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 40
    • 0028246440 scopus 로고
    • Binding of G protein βγ-subunits to pleckstrin homology domains
    • Touhara, K., Inglese, J., Pitcher, J. A., Shaw, G. and Lafkowitz, R. J. (1994). Binding of G protein βγ-subunits to pleckstrin homology domains. J Biol. Chem. 269, 10217-10220.
    • (1994) J Biol. Chem. , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lafkowitz, R.J.5
  • 41
    • 0028173394 scopus 로고
    • Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada, S., Simon, M. I., Witte, O. N. and Katz, A. (1994) Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc. Natl Acad Sci. USA 91, 11256-11260.
    • (1994) Proc. Natl Acad Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 43
    • 0028093610 scopus 로고
    • CRAC, a cytosolic protein containing a pleckstrin homology domain, is required for receptor and G protein-mediated activation of adenylyl cyclase in Dictyostelium
    • Insall, R. et al. (1994). CRAC, a cytosolic protein containing a pleckstrin homology domain, is required for receptor and G protein-mediated activation of adenylyl cyclase in Dictyostelium. J Cell Biol. 126, 1537-1545.
    • (1994) J Cell Biol. , vol.126 , pp. 1537-1545
    • Insall, R.1
  • 44
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • Crespo, P., Xu, N., Simonds, W. F. and Gutkind, J. S. (1994). Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits. Nature 369, 418-420.
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 45
    • 0028977847 scopus 로고
    • Receptor-tyrosine-kinase- And Gβγ-meditated MAP kinase activation by a common signalling pathway
    • van Biesen, T. et al. (1995). Receptor-tyrosine-kinase- and Gβγ-meditated MAP kinase activation by a common signalling pathway Nature 376, 781-784.
    • (1995) Nature , vol.376 , pp. 781-784
    • Van Biesen, T.1
  • 46
    • 0028064275 scopus 로고
    • Binding of PH domains of β-adrenergic receptor kinase and β-spectrin to WD40/β-transducin repeat containing regions of the β-subunit of trimeric G-proteins
    • Wang, D. S., Shaw, R., Winkelmann, J. C. and Shaw, G. (1994). Binding of PH domains of β-adrenergic receptor kinase and β-spectrin to WD40/β-transducin repeat containing regions of the β-subunit of trimeric G-proteins. Biochem. Biophys. Res. Commun 203, 29-35.
    • (1994) Biochem. Biophys. Res. Commun , vol.203 , pp. 29-35
    • Wang, D.S.1    Shaw, R.2    Winkelmann, J.C.3    Shaw, G.4
  • 47
    • 0028904974 scopus 로고
    • Binding of pleckstrin homology domains to WD40/β-transducin repeat containing segments of the protein product of the Lis-1 gene
    • Wang, D. S., Shaw, R., Hattori, M., Arai, H., Inoue, K. and Shaw, G. (1995). Binding of pleckstrin homology domains to WD40/β-transducin repeat containing segments of the protein product of the Lis-1 gene. Biochem. Biophys. Res. Commun. 209, 622-629.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 622-629
    • Wang, D.S.1    Shaw, R.2    Hattori, M.3    Arai, H.4    Inoue, K.5    Shaw, G.6
  • 48
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E. J., Schmidt, C. J., Nambudripad, R. and Smith, T. F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 49
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: A homolog of the β subunit of G proteins
    • Ron, D., Chen, C.-H., Caldwell, J., Jamieson, L., Orr, E. and Mochly-Rosen, D. (1994). Cloning of an intracellular receptor for protein kinase C: a homolog of the β subunit of G proteins. Proc. Natl. Acad. Sci. USA 91, 839-843.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 839-843
    • Ron, D.1    Chen, C.-H.2    Caldwell, J.3    Jamieson, L.4    Orr, E.5    Mochly-Rosen, D.6
  • 50
    • 0028564915 scopus 로고
    • The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C
    • Yao, L., Kawakami, Y. and Kawakami, T. (1994). The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. Proc. Natl Acad. Sci. USA 91, 9175-9179.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9175-9179
    • Yao, L.1    Kawakami, Y.2    Kawakami, T.3
  • 51
    • 0028670203 scopus 로고
    • The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase Cζ
    • Konishi, H., Kuroda, S. and Kikkawa, U. (1994). The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase Cζ. Biochem. Biophys. Res. Commun. 205, 1770-1775.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1770-1775
    • Konishi, H.1    Kuroda, S.2    Kikkawa, U.3
  • 52
    • 0027985080 scopus 로고
    • Molecular cloning of rat RAC protein kinase α and β and their association with protein kinase Cζ
    • Konishi, H., Shinomura, T., Kuroda, S., Ono, Y. and Kikkawa, U. (1994). Molecular cloning of rat RAC protein kinase α and β and their association with protein kinase Cζ. Biochem. Biophys. Res. Commun. 205, 817-825.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 817-825
    • Konishi, H.1    Shinomura, T.2    Kuroda, S.3    Ono, Y.4    Kikkawa, U.5
  • 53
    • 0026703004 scopus 로고
    • Putative inositol 1,4,5-triphosphate binding proteins in rat brain cytosol
    • Kanematsu, T. et al. (1992). Putative inositol 1,4,5-triphosphate binding proteins in rat brain cytosol. J. Biol. Chem. 267, 6518-6525.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6518-6525
    • Kanematsu, T.1
  • 54
    • 0028132554 scopus 로고
    • Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phoshatidylinositol-specific phospholipase C-δ1
    • Yagisawa, H. et al. (1994). Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phoshatidylinositol-specific phospholipase C-δ1. J. Biol. Chem. 269, 20179-20188.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20179-20188
    • Yagisawa, H.1
  • 55
    • 0027310309 scopus 로고
    • Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1: Catalytic and membrane binding properties
    • Cifuentes, M. E., Honkanan, L. and Rabecchi, M. J. (1993). Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1: catalytic and membrane binding properties. J. Biol. Chem. 268, 11586-11593.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11586-11593
    • Cifuentes, M.E.1    Honkanan, L.2    Rabecchi, M.J.3
  • 56
    • 0028040136 scopus 로고
    • D-myo-inositol 1,4,5-trisphosphate inhibits binding of phospholipase C-δ1 to bilayer membranes
    • Cifuentes, M. E., Delaney, T. and Rebecchi, M. J. (1994). D-myo-inositol 1,4,5-trisphosphate inhibits binding of phospholipase C-δ1 to bilayer membranes. J. Biol. Chem. 269, 1945-1948.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1945-1948
    • Cifuentes, M.E.1    Delaney, T.2    Rebecchi, M.J.3
  • 57
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J. E., Hajduk, P. J., Yoon, H. S. and Fesik, S. W. (1994). Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 58
    • 0028169731 scopus 로고
    • G spectrin that bind to distinct sites in brain membranes
    • G spectrin that bind to distinct sites in brain membranes. J. Biol. Chem. 269, 4409-4416.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4409-4416
    • Davis, L.H.1    Bennett, V.2
  • 59
    • 0028172233 scopus 로고
    • II-spectrin (fodrin) and βIε2-spectrin (muscle) contain NH2- And COOH-teminal membrane association domains (MAD1 and MAD2)
    • Lombardo, C. R., Weed, S. A., Kennedy, S. P., Forget, B. G. and Morrow, J. S. (1994). βII-spectrin (fodrin) and βIε2-spectrin (muscle) contain NH2- and COOH-teminal membrane association domains (MAD1 and MAD2). J. Biol. Chem. 289, 29212-29219.
    • (1994) J. Biol. Chem. , vol.289 , pp. 29212-29219
    • Lombardo, C.R.1    Weed, S.A.2    Kennedy, S.P.3    Forget, B.G.4    Morrow, J.S.5
  • 62
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. H. and Coffer, P. J. (1995). Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376, 599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.H.1    Coffer, P.J.2
  • 63
    • 0029055503 scopus 로고
    • Pleckstrin inhibits phosphoinositide hydrolysis initiated by G-protein-coupled and growth factor receptors
    • Abrams, C. S., Wu, H., Zhao, W., Belmonte, E., White,D. and Brass, L. F. (1995). Pleckstrin inhibits phosphoinositide hydrolysis initiated by G-protein-coupled and growth factor receptors. J. Biol. Chem. 270, 14485-14492.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14485-14492
    • Abrams, C.S.1    Wu, H.2    Zhao, W.3    Belmonte, E.4    White, D.5    Brass, L.F.6
  • 65
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the β-adrenergic receptor kinase requires coordinate interaction with Gβγ subunits and lipid
    • Pitcher, J. A., Touhara, K., Payne, E. S. and Lefkowitz, R. J. (1995). Pleckstrin homology domain-mediated membrane association and activation of the β-adrenergic receptor kinase requires coordinate interaction with Gβγ subunits and lipid. J. Biol. Chem. 270, 11707-11710.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 66
    • 0028891875 scopus 로고
    • Mutational Analysis of the Pleckstrin Homology Domain of the β-Adrenergic Receptor Kinase
    • Touhara, K., Koch, W. J., Hawes, B. E. and Lefkowitz, R. J. (1995). Mutational Analysis of the Pleckstrin Homology Domain of the β-Adrenergic Receptor Kinase. J. Biol. Chem. 270, 17000-17005.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17000-17005
    • Touhara, K.1    Koch, W.J.2    Hawes, B.E.3    Lefkowitz, R.J.4
  • 67
    • 0027185782 scopus 로고
    • Mechanism of β-Adrenergic receptor kinase activation by G proteins
    • Kim, C. M., Dion, S. B. and Benovic, J. L. (1993). Mechanism of β-Adrenergic receptor kinase activation by G proteins J. Biol. Chem. 268, 15412-15418.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15412-15418
    • Kim, C.M.1    Dion, S.B.2    Benovic, J.L.3
  • 68
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting, C. P. and Phillips, C. S. O. (1995). DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem. Sci. 20, 102-103.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.S.O.2
  • 69
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S. and McCormick, F. (1993). Proteins regulating Ras and its relatives. Nature 366, 643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2


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