메뉴 건너뛰기




Volumn 34, Issue 4, 1999, Pages 215-251

Whither goest the RGS proteins?

Author keywords

Desensitization, effector proteins; GGL; GoLoco; PDZ; PTB; Regulators of G protein signaling; RGS; Scaffold proteins; Signal transduction

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PHEROMONE; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE; REGULATOR PROTEIN;

EID: 0032863252     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409239991209273     Document Type: Review
Times cited : (97)

References (176)
  • 2
    • 0032492722 scopus 로고    scopus 로고
    • Sst2 is a GTPase-activating protein for Gpa1: Purification and characterization of a cognate RGS-Galpha protein pair in yeast
    • Apanovitch, D. M., Slep, K. C., Sigler, P. B., and Dohlman, H. G. 1998. Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Galpha protein pair in yeast. Biochemistry 37: 4815-22.
    • (1998) Biochemistry , vol.37 , pp. 4815-4822
    • Apanovitch, D.M.1    Slep, K.C.2    Sigler, P.B.3    Dohlman, H.G.4
  • 3
    • 0031910742 scopus 로고    scopus 로고
    • Lifetime regulation of G protein-effector complex: Emerging importance of RGS proteins
    • Arshavsky, V. Y. and Pugh, E. N., Jr. 1998. Lifetime regulation of G protein-effector complex: emerging importance of RGS proteins. Neuron 20: 11-4.
    • (1998) Neuron , vol.20 , pp. 11-14
    • Arshavsky, V.Y.1    Pugh Jr., E.N.2
  • 4
    • 0032529161 scopus 로고    scopus 로고
    • Differential recruitment of Dishevelled provides signaling specificity in the planar cell polarity and Wingless signaling pathways
    • Axelrod, J. D., Miller, J. R., Shulman, J. M., Moon, R. T., and Perrimon, N. 1998. Differential recruitment of Dishevelled provides signaling specificity in the planar cell polarity and Wingless signaling pathways. Genes Dev. 12:2610-22.
    • (1998) Genes Dev. , vol.12 , pp. 2610-2622
    • Axelrod, J.D.1    Miller, J.R.2    Shulman, J.M.3    Moon, R.T.4    Perrimon, N.5
  • 5
    • 0031770289 scopus 로고    scopus 로고
    • Frizzled proteins constitute a novel family of G protein-coupled receptors, most closely related to the secretin family
    • Barnes, M. R., Duckworth, D. M., and Beeley, L. J. 1998. Frizzled proteins constitute a novel family of G protein-coupled receptors, most closely related to the secretin family. Trends Pharmacol. Sci. 19: 399-400.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 399-400
    • Barnes, M.R.1    Duckworth, D.M.2    Beeley, L.J.3
  • 9
    • 0031916822 scopus 로고    scopus 로고
    • Mammalian RGS proteins: Barbarians at the gate
    • Berman, D. M. and Gilman, A. G. 1998. Mammalian RGS proteins: barbarians at the gate. J. Biol. Chem. 273: 1269-72.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1269-1272
    • Berman, D.M.1    Gilman, A.G.2
  • 10
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits
    • Berman, D. M., Wilkie, T. M., and Gilman, A. G. 1996. GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits. Cell 86: 445-52.
    • (1996) Cell , vol.86 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 11
    • 0026694917 scopus 로고
    • Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator
    • Berstein, G., Blank, J. L., Jhon, D.-Y., Exton, J. H., Rhee, S. G., and Ross, E. M. 1992. Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator. Cell 70: 411-8.
    • (1992) Cell , vol.70 , pp. 411-418
    • Berstein, G.1    Blank, J.L.2    Jhon, D.-Y.3    Exton, J.H.4    Rhee, S.G.5    Ross, E.M.6
  • 12
    • 0029961069 scopus 로고    scopus 로고
    • Regulation of phospholipase C-beta 1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation
    • Biddlecome, G. H., Berstein, G., and Ross, E. M. 1996. Regulation of phospholipase C-beta 1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation. J. Biol. Chem. 271:7999-8007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7999-8007
    • Biddlecome, G.H.1    Berstein, G.2    Ross, E.M.3
  • 13
    • 0028568639 scopus 로고
    • A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie, P., Immanuel, D., Wu, J., Li, N., Yajnik, V., and Margolis, B. 1994. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269: 32031-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1    Immanuel, D.2    Wu, J.3    Li, N.4    Yajnik, V.5    Margolis, B.6
  • 14
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg, J. P., Ooi, J., Levy, E., and Margolis, B. 1996. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16: 6229-41.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 15
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne, H. R. 1997. How receptors talk to trimeric G proteins. Curr. Biol. 9: 134-42.
    • (1997) Curr. Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 16
    • 0032561305 scopus 로고    scopus 로고
    • Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members
    • Bowman, E. P., Campbell, J. J., Druey, K. M., Scheschonka, A., Kehrl, J. H., and Butcher, E. C. 1998. Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members. J. Biol. Chem. 273: 28040-8.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28040-28048
    • Bowman, E.P.1    Campbell, J.J.2    Druey, K.M.3    Scheschonka, A.4    Kehrl, J.H.5    Butcher, E.C.6
  • 17
    • 0026697940 scopus 로고
    • Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin
    • Brown, N. G., Fowles, C., Sharma, R., and Akhtar, M. 1992. Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin. Eur J. Biochem. 208: 659-67.
    • (1992) Eur J. Biochem. , vol.208 , pp. 659-667
    • Brown, N.G.1    Fowles, C.2    Sharma, R.3    Akhtar, M.4
  • 19
    • 0031456158 scopus 로고    scopus 로고
    • Wnt signaling: A common theme in animal development
    • Cadigan, K. M. and Nusse, R. 1997. Wnt signaling: a common theme in animal development. Genes Dev. 11: 3286-305.
    • (1997) Genes Dev. , vol.11 , pp. 3286-3305
    • Cadigan, K.M.1    Nusse, R.2
  • 20
    • 0032493759 scopus 로고    scopus 로고
    • Binding and phosphorylation of tubulin by G protein-coupled receptor kinases
    • Carman, C. V., Som, T., Kim, C. M., and Benovic, J. L. 1998. Binding and phosphorylation of tubulin by G protein-coupled receptor kinases. J. Biol. Chem. 273: 20308-16.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20308-20316
    • Carman, C.V.1    Som, T.2    Kim, C.M.3    Benovic, J.L.4
  • 21
    • 0020040057 scopus 로고
    • Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones
    • Chan, R. K. and Otte, C. A. 1982a. Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol. Cell. Biol. 2: 11-20.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 11-20
    • Chan, R.K.1    Otte, C.A.2
  • 22
    • 0020039329 scopus 로고
    • Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones
    • Chan, R. K. and Otte, C. A. 1982b. Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol. Cell. Biol. 2: 21-9.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 21-29
    • Chan, R.K.1    Otte, C.A.2
  • 23
    • 0029988340 scopus 로고    scopus 로고
    • Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity
    • Charest, A., Wagner, J., Jacob, S., McGlade, C. J., and Tremblay, M. L. 1996. Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity. J. Biol. Chem. 271: 8424-9.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8424-8429
    • Charest, A.1    Wagner, J.2    Jacob, S.3    McGlade, C.J.4    Tremblay, M.L.5
  • 24
    • 0031006273 scopus 로고    scopus 로고
    • A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C
    • Chatterjee, T. K., Eapen, A. K., and Fisher, R. A. 1997. A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C. J. Biol. Chem. 272: 15481-7.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15481-15487
    • Chatterjee, T.K.1    Eapen, A.K.2    Fisher, R.A.3
  • 25
    • 0033538337 scopus 로고    scopus 로고
    • Phospholipase C-beta 1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbetagamma subunits
    • Chidiac, P. and Ross, E. M. 1999. Phospholipase C-beta 1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbetagamma subunits. J. Biol. Chem. 274: 19639-19643.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19639-19643
    • Chidiac, P.1    Ross, E.M.2
  • 27
    • 0033546001 scopus 로고    scopus 로고
    • Structure of Gialpha1-GppNHp, autoinhibition in a Galpha protein-substrate complex
    • Coleman, D. E. and Sprang, S. R. 1999. Structure of Gialpha1-GppNHp, autoinhibition in a Galpha protein-substrate complex. J. Biol. Chem. 274: 16669-72.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16669-16672
    • Coleman, D.E.1    Sprang, S.R.2
  • 28
    • 0032574719 scopus 로고    scopus 로고
    • High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods
    • Cowan, C. W., Fariss, R. N., Sokal, I., Palczewski, K., and Wensel, T. G. 1998. High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods. Proc. Natl. Acad. Sci. U.S.A. 95: 5351-6.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5351-5356
    • Cowan, C.W.1    Fariss, R.N.2    Sokal, I.3    Palczewski, K.4    Wensel, T.G.5
  • 29
    • 0032510020 scopus 로고    scopus 로고
    • Wingless signaling: The inconvenient complexities of life
    • Cox, R. T. and Peifer, M. 1998. Wingless signaling: the inconvenient complexities of life. Curr. Biol. 8: R140-R144.
    • (1998) Curr. Biol. , vol.8
    • Cox, R.T.1    Peifer, M.2
  • 30
    • 0032524629 scopus 로고    scopus 로고
    • PDZ proteins organize synaptic signaling pathways
    • Craven, S. E. and Bredt, D. S. 1998. PDZ proteins organize synaptic signaling pathways. Cell 93: 495-8.
    • (1998) Cell , vol.93 , pp. 495-498
    • Craven, S.E.1    Bredt, D.S.2
  • 31
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein beta/ gamma subunits
    • Crespo, P., Xu, N., Simonds, W. F., and Gutkind, J. S. 1994. Ras-dependent activation of MAP kinase pathway mediated by G-protein beta/ gamma subunits. Nature 369: 418-20.
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 32
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • Daub, H., Wallasch, C., Lankenau, A., Herrlich, A., and Ullrich, A. 1997. Signal characteristics of G protein-transactivated EGF receptor. EMBO J. 16: 7032-44.
    • (1997) EMBO J. , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3    Herrlich, A.4    Ullrich, A.5
  • 33
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub, H., Weiss, F. U., Wallasch, C., and Ullrich, A. 1996. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 379: 557-60.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich, A.4
  • 34
    • 0344528755 scopus 로고    scopus 로고
    • RGS proteins: More than just GAPs for heterotrimeric G proteins
    • De Vries, L. and Farquhar, M. G. 1999. RGS proteins: more than just GAPs for heterotrimeric G proteins. Trends Cell. Biol. 9: 138-44.
    • (1999) Trends Cell. Biol. , vol.9 , pp. 138-144
    • De Vries, L.1    Farquhar, M.G.2
  • 35
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein G-alpha i3, is a member of a protein family with a highly conserved core domain
    • De Vries, L., Mousli, M., Wurmser, A., and Farquhar, M. G. 1995. GAIP, a protein that specifically interacts with the trimeric G protein G-alpha i3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. U.S.A. 92: 11916-20.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 36
    • 0033553526 scopus 로고    scopus 로고
    • Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases
    • Della Rocca, G. J., Maudsley, S., Daaka, Y., Lefkowitz, R. J., and Luttrell, L. M. 1999. Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases. J. Biol. Chem. 274: 13978-84.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13978-13984
    • Della Rocca, G.J.1    Maudsley, S.2    Daaka, Y.3    Lefkowitz, R.J.4    Luttrell, L.M.5
  • 37
    • 0030872062 scopus 로고    scopus 로고
    • Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors. Convergence of Gi- and Gq-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase
    • Della Rocca, G. J., van Biesen, T., Daaka, Y., Luttrell, D. K., Luttrell, L. M., and Lefkowitz, R. J. 1997. Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors. Convergence of Gi- and Gq-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase. J. Biol. Chem. 272: 19125-32.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19125-19132
    • Della Rocca, G.J.1    Van Biesen, T.2    Daaka, Y.3    Luttrell, D.K.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 38
    • 0032502726 scopus 로고    scopus 로고
    • The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX
    • Dho, S. E., Jacob, S., Wolting, C. D., French, M. B., Rohrschneider, L. R., and McGlade, C. J. 1998. The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX. J. Biol. Chem. 273: 9179-87.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9179-9187
    • Dho, S.E.1    Jacob, S.2    Wolting, C.D.3    French, M.B.4    Rohrschneider, L.R.5    McGlade, C.J.6
  • 39
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic, I., Tokiwa, G., Lev, S., Courtneidge, S. A., and Schlessinger, J. 1996. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383: 547-50.
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 41
    • 0029058433 scopus 로고
    • Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae
    • Dohlman, H. G., Apaniesk, D., Chen, Y., Song, J., and Nusskern, D. 1995. Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae. Mol. Cell. Biol. 15: 3635-43.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3635-3643
    • Dohlman, H.G.1    Apaniesk, D.2    Chen, Y.3    Song, J.4    Nusskern, D.5
  • 43
    • 0031041306 scopus 로고    scopus 로고
    • RGS proteins and signaling by heterotrimeric G proteins
    • Dohlman, H. G. and Thorner, J. 1997. RGS proteins and signaling by heterotrimeric G proteins. J. Biol. Chem. 272: 3871-4.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3871-3874
    • Dohlman, H.G.1    Thorner, J.2
  • 44
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D. A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85: 1067-76.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 45
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey, K. M., Blumer, K. J., Kang, V. H., and Kehrl, J. H. 1996. Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. Nature 379: 742-6.
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 47
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS - 1 PTB domain bound to the juxtamembrane region of the insulin receptor
    • Eck, M. J., Dhe-Paganon, S., Trub, T., Nolte, R. T., and Shoelson, S. E. 1996. Structure of the IRS - 1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell 85: 695-705.
    • (1996) Cell , vol.85 , pp. 695-705
    • Eck, M.J.1    Dhe-Paganon, S.2    Trub, T.3    Nolte, R.T.4    Shoelson, S.E.5
  • 48
    • 0030293766 scopus 로고    scopus 로고
    • Protein-protein interactions: PDZ domain networks
    • Fanning, A. S. and Anderson, J. M. 1996. Protein-protein interactions: PDZ domain networks. Curr. Biol. 6: 1385-8.
    • (1996) Curr. Biol. , vol.6 , pp. 1385-1388
    • Fanning, A.S.1    Anderson, J.M.2
  • 49
    • 0028176297 scopus 로고
    • cAMP and beta/gamma subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells
    • Faure, M., Voyno-Yasenetskaya, T. A., and Bourne, H. R. 1994. cAMP and beta/gamma subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells. J. Biol. Chem. 269: 7851-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7851-7854
    • Faure, M.1    Voyno-Yasenetskaya, T.A.2    Bourne, H.R.3
  • 51
    • 0032563208 scopus 로고    scopus 로고
    • Different regions of Rho determine Rho-selective binding of different classes of Rho target molecules
    • Fujisawa, K., Madaule, P., Ishizaki, T., Watanabe, G., Bito, H., Saito, Y., Hall, A., and Narumiya, S. 1998. Different regions of Rho determine Rho-selective binding of different classes of Rho target molecules. J. Biol. Chem. 273: 18943-9.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18943-18949
    • Fujisawa, K.1    Madaule, P.2    Ishizaki, T.3    Watanabe, G.4    Bito, H.5    Saito, Y.6    Hall, A.7    Narumiya, S.8
  • 52
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
    • Fukuhara, S., Murga, C., Zohar, M., Igishi, T., and Gutkind, J. S. 1999. A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho. J. Biol. Chem. 274: 5868-79.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5868-5879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3    Igishi, T.4    Gutkind, J.S.5
  • 53
    • 0024338902 scopus 로고
    • Drosophila abl tyrosine kinase in embryonic CNS axons: A role in axonogenesis is revealed through dosage-sensitive interactions with disabled
    • Gertler, F. B., Bennett, R. L., Clark, M. J., and Hoffmann, F. M. 1989. Drosophila abl tyrosine kinase in embryonic CNS axons: a role in axonogenesis is revealed through dosage-sensitive interactions with disabled. Cell 58: 103-13.
    • (1989) Cell , vol.58 , pp. 103-113
    • Gertler, F.B.1    Bennett, R.L.2    Clark, M.J.3    Hoffmann, F.M.4
  • 54
    • 0027245960 scopus 로고
    • Dosage-sensitive modifiers of Drosophila abl tyrosine kinase function: Prospero, a regulator of axonal outgrowth, and disabled, a novel tyrosine kinase substrate
    • Gertler, F. B., Hill, K. K., Clark, M. J., and Hoffmann, F. M. 1993. Dosage-sensitive modifiers of Drosophila abl tyrosine kinase function: prospero, a regulator of axonal outgrowth, and disabled, a novel tyrosine kinase substrate. Genes Dev. 7: 441-53.
    • (1993) Genes Dev. , vol.7 , pp. 441-453
    • Gertler, F.B.1    Hill, K.K.2    Clark, M.J.3    Hoffmann, F.M.4
  • 55
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A. G. 1987. G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56: 615-49.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 56
    • 0002671971 scopus 로고
    • The effects of a lethal mutation responsible for duplications and twinning in mouse embryos
    • Glückson-Schönheimer, S. 1949. The effects of a lethal mutation responsible for duplications and twinning in mouse embryos. J. Exp. Zool. 100: 47-76.
    • (1949) J. Exp. Zool. , vol.100 , pp. 47-76
    • Glückson-Schönheimer, S.1
  • 58
    • 0031782937 scopus 로고    scopus 로고
    • Molecular characterization of human and rat RGS 9L, a novel splice variant enriched in dopamine target regions, and chromosomal localization of the RGS 9 gene
    • Granneman, J. G., Zhai, Y., Zhu, Z., Bannon, M. J., Burchett, S. A., Schmidt, C. J., Andrade, R., and Cooper, J. 1998. Molecular characterization of human and rat RGS 9L, a novel splice variant enriched in dopamine target regions, and chromosomal localization of the RGS 9 gene. Mol. Pharm. 54: 687-694.
    • (1998) Mol. Pharm. , vol.54 , pp. 687-694
    • Granneman, J.G.1    Zhai, Y.2    Zhu, Z.3    Bannon, M.J.4    Burchett, S.A.5    Schmidt, C.J.6    Andrade, R.7    Cooper, J.8
  • 59
    • 0026441231 scopus 로고
    • Activation of transforming G protein-coupled receptors induces rapid tyrosine phosphorylation of cellular proteins, including p125FAK and the p130 v-src substrate
    • Gutkind, J. S. and Robbins, K. C. 1992. Activation of transforming G protein-coupled receptors induces rapid tyrosine phosphorylation of cellular proteins, including p125FAK and the p130 v-src substrate. Biochem. Biophys. Res. Commun. 188: 155-61.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 155-161
    • Gutkind, J.S.1    Robbins, K.C.2
  • 60
    • 0032528248 scopus 로고    scopus 로고
    • GTP-binding-protein-coupled receptor kinase 2 (GRK2) binds and phosphorylates tubulin
    • Haga, K., Ogawa, H., Haga, T., and Murofushi, H. 1998. GTP-binding-protein-coupled receptor kinase 2 (GRK2) binds and phosphorylates tubulin. Eur. J. Biochem. 255: 363-8.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 363-368
    • Haga, K.1    Ogawa, H.2    Haga, T.3    Murofushi, H.4
  • 61
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell. Biol. 10: 31-54.
    • (1994) Annu. Rev. Cell. Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 62
    • 0032555156 scopus 로고    scopus 로고
    • A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins
    • Hall, R. A., Ostedgaard, L. S., Premont, R. T., Blitzer, J. T., Rahman, N., Welsh, M. J., and Lefkowitz, R. J. 1998a. A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins. Proc. Natl. Acad. Sci. U.S.A. 95: 8496-501.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8496-8501
    • Hall, R.A.1    Ostedgaard, L.S.2    Premont, R.T.3    Blitzer, J.T.4    Rahman, N.5    Welsh, M.J.6    Lefkowitz, R.J.7
  • 64
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm, H. E. 1998. The many faces of G protein signaling. J. Biol. Chem. 273: 669-72.
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 65
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison, S. C. 1996. Peptide-surface association: the case of PDZ and PTB domains. Cell 86: 341-3.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 66
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3beta
    • Hart, M. J., de los Santos, R., Albert, I. N., Rubinfeld, B., and Polakis, P. 1998a. Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3beta. Curr. Biol. 8: 573-81.
    • (1998) Curr. Biol. , vol.8 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 67
    • 0027958423 scopus 로고
    • Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
    • Hart, M. J., Eva, A., Zangrilli, D., Aaronson, S. A., Evans, T., Cerione, R. A., and Zheng, Y. 1994. Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem. 269: 62-5.
    • (1994) J. Biol. Chem. , vol.269 , pp. 62-65
    • Hart, M.J.1    Eva, A.2    Zangrilli, D.3    Aaronson, S.A.4    Evans, T.5    Cerione, R.A.6    Zheng, Y.7
  • 69
  • 70
    • 0031936503 scopus 로고    scopus 로고
    • RGS9, a GTPase accelerator for phototransduction
    • He, W., Cowan, C. W., and Wensel, T. G. 1998. RGS9, a GTPase accelerator for phototransduction. Neuron 20: 95-102.
    • (1998) Neuron , vol.20 , pp. 95-102
    • He, W.1    Cowan, C.W.2    Wensel, T.G.3
  • 71
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha
    • Hepler, J. R., Berman, D. M., Gilman, A. G., and Kozasa, T. 1997. RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha. Proc. Natl. Acad. Sci. U.S.A. 94: 428-32.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, D.M.2    Gilman, A.G.3    Kozasa, T.4
  • 72
    • 0032555202 scopus 로고    scopus 로고
    • Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic, acid-stimulated mitogenic activity in L cells
    • Herrlich, A., Daub, H., Knebel, A., Herrlich, P., Ullrich, A., Schultz, G., and Gudermann, T. 1998. Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic, acid-stimulated mitogenic activity in L cells. Proc. Natl. Acad. Sci. U.S.A. 95: 8985-90.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8985-8990
    • Herrlich, A.1    Daub, H.2    Knebel, A.3    Herrlich, P.4    Ullrich, A.5    Schultz, G.6    Gudermann, T.7
  • 73
    • 0027530675 scopus 로고
    • A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor
    • Heximer, S. P. and Forsdyke, D. R. 1993. A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor. DNA Cell. Biol. 12: 73-88.
    • (1993) DNA Cell. Biol. , vol.12 , pp. 73-88
    • Heximer, S.P.1    Forsdyke, D.R.2
  • 74
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • Hillier, B. J., Christopherson, K. S., Prehoda, K. E., Bredt, D. S., and Lim, W. A. 1999. Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284: 812-5.
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 75
    • 0027958335 scopus 로고
    • Transfected platelet-activating factor receptor activates mitogen-activated protein (MAP) kinase and MAP kinase kinase in Chinese hamster ovary cells
    • Honda, Z., Takano, T., Gotoh, Y., Nishida, E., Ito, K., and Shimizu, T. 1994. Transfected platelet-activating factor receptor activates mitogen-activated protein (MAP) kinase and MAP kinase kinase in Chinese hamster ovary cells. J. Biol. Chem. 269: 2307-2315.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2307-2315
    • Honda, Z.1    Takano, T.2    Gotoh, Y.3    Nishida, E.4    Ito, K.5    Shimizu, T.6
  • 76
    • 0027253487 scopus 로고
    • Isolation and characterization of a novel B cell activation gene
    • Hong, J. X., Wilson, G. L., Fox, C. H., and Kehrl, J. H. 1993. Isolation and characterization of a novel B cell activation gene. J. Immunol. 150: 3895-904.
    • (1993) J. Immunol. , vol.150 , pp. 3895-3904
    • Hong, J.X.1    Wilson, G.L.2    Fox, C.H.3    Kehrl, J.H.4
  • 77
    • 0031035703 scopus 로고    scopus 로고
    • Mouse disabled (mDab1): A Src binding protein implicated in neuronal development
    • Howell, B. W., Gertler, F. B., and Cooper, J. A. 1997. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO J. 16: 121-32.
    • (1997) EMBO J. , vol.16 , pp. 121-132
    • Howell, B.W.1    Gertler, F.B.2    Cooper, J.A.3
  • 78
    • 0033066680 scopus 로고    scopus 로고
    • The Disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell, B. W., Lanier, L. M., Frank, R., Gertler, F. B., and Cooper, J. A. 1999. The Disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19: 5179-88.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 79
    • 0030610240 scopus 로고    scopus 로고
    • Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells
    • Huang, C., Hepler, J. R., Gilman, A. G., and Mumby, S. M. 1997. Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 94: 6159-63.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6159-6163
    • Huang, C.1    Hepler, J.R.2    Gilman, A.G.3    Mumby, S.M.4
  • 80
  • 81
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits
    • Huang, L. J., Durick, K., Weiner, J. A., Chun, J., and Taylor, S. S. 1997b. Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J. Biol. Chem. 272: 8057-64.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8057-8064
    • Huang, L.J.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 82
    • 0032489284 scopus 로고    scopus 로고
    • Tyrosine kinases of the Src family participate in signaling to MAP kinase from both Gq and Gi-coupled receptors
    • Igishi, T. and Gutkind, J. S. 1998. Tyrosine kinases of the Src family participate in signaling to MAP kinase from both Gq and Gi-coupled receptors. Biochem. Biophys. Res. Commun. 244: 5-10.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 5-10
    • Igishi, T.1    Gutkind, J.S.2
  • 83
    • 0032473355 scopus 로고    scopus 로고
    • Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin
    • Ikeda, S., Kishida, S., Yamamoto, H., Murai, H., Koyama, S., and Kikuchi, A. 1998. Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin. Embo J. 17: 1371-84.
    • (1998) Embo J. , vol.17 , pp. 1371-1384
    • Ikeda, S.1    Kishida, S.2    Yamamoto, H.3    Murai, H.4    Koyama, S.5    Kikuchi, A.6
  • 84
    • 0027368165 scopus 로고
    • Structure and mechanism of the G protein-coupled receptor kinases
    • Inglese, J., Freedman, N. J., Koch, W. J., and Lefkowitz, R. J. 1993. Structure and mechanism of the G protein-coupled receptor kinases. J. Biol. Chem. 268: 23735-8.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 85
    • 0032493042 scopus 로고    scopus 로고
    • Axis determination in Xenopus involves biochemical interactions of axin, glycogen synthase kinase 3 and beta-catenin
    • Itoh, K., Krupnik, V. E., and Sokol, S. Y. 1998. Axis determination in Xenopus involves biochemical interactions of axin, glycogen synthase kinase 3 and beta-catenin. Curr. Biol. 8: 591-4.
    • (1998) Curr. Biol. , vol.8 , pp. 591-594
    • Itoh, K.1    Krupnik, V.E.2    Sokol, S.Y.3
  • 87
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, W. M. and Williams, L. T. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266: 1862-5.
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 89
    • 0032079884 scopus 로고    scopus 로고
    • Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of beta-catenin
    • Kishida, S., Yamamoto, H., Ikeda, S., Kishida, M., Sakamoto, I., Koyama, S., and Kikuchi, A. 1998. Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of beta-catenin. J. Biol. Chem. 273: 10823-6.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10823-10826
    • Kishida, S.1    Yamamoto, H.2    Ikeda, S.3    Kishida, M.4    Sakamoto, I.5    Koyama, S.6    Kikuchi, A.7
  • 90
    • 0028670476 scopus 로고
    • Direct evidence that Gi-coupled receptor stimulation of mitogen-activated protein kinase is mediated by G beta gamma activation of p21ras
    • Koch, W. J., Hawes, B. E., Allen, L. F., and Lefkowitz, R. J. 1994. Direct evidence that Gi-coupled receptor stimulation of mitogen-activated protein kinase is mediated by G beta gamma activation of p21ras. Proc. Natl. Acad. Sci. U.S.A. 91: 12706-10.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12706-12710
    • Koch, W.J.1    Hawes, B.E.2    Allen, L.F.3    Lefkowitz, R.J.4
  • 91
    • 0030907376 scopus 로고    scopus 로고
    • A new family of G-protein regulators - The RGS proteins
    • Koelle, M. R. 1997. A new family of G-protein regulators - the RGS proteins. Curr. Opin. Cell Biol. 9: 143-7.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 143-147
    • Koelle, M.R.1
  • 92
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
    • Koelle, M. R., and Horvitz, H. R. 1996. EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84: 115-25.
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 94
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • Krupnick, J. G. and Benovic, J. L. 1998. The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu. Rev. Pharmacol. Toxicol 38: 289-319.
    • (1998) Annu. Rev. Pharmacol. Toxicol , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 95
    • 0027144459 scopus 로고
    • The pheromone response pathway in Saccharomyces cerevisiae
    • Kurjan, J. 1993. The pheromone response pathway in Saccharomyces cerevisiae. Annu. Rev. Genet. 27: 147-179.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 147-179
    • Kurjan, J.1
  • 96
    • 0031876218 scopus 로고    scopus 로고
    • Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase
    • Le, N. and Simon, M. A. 1998. Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase. Mol. Cell. Biol. 18: 4844-54.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4844-4854
    • Le, N.1    Simon, M.A.2
  • 97
    • 0028139212 scopus 로고
    • Overexpression of flbA, an early regulator of Aspergillus asexual sporulation, leads to activation of brlA and premature initiation of development
    • Lee, B. N. and Adams, T. H. 1994. Overexpression of flbA, an early regulator of Aspergillus asexual sporulation, leads to activation of brlA and premature initiation of development. Mol. Microbiol. 14: 323-34.
    • (1994) Mol. Microbiol. , vol.14 , pp. 323-334
    • Lee, B.N.1    Adams, T.H.2
  • 98
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M. A., Ferguson, K. M., and Schlessinger, J. 1996. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85: 621-4.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 99
    • 0033514516 scopus 로고    scopus 로고
    • Gbeta5 prevents the RGS7-Galpha-o interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins
    • Levay, K., Cabrera, J. L., Satpaev, D. K., and Slepak, V. Z. 1999. Gbeta5 prevents the RGS7-Galpha-o interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins. Proc. Natl. Acad. Sci. U.S.A. 96: 2503-7.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2503-2507
    • Levay, K.1    Cabrera, J.L.2    Satpaev, D.K.3    Slepak, V.Z.4
  • 101
    • 0032568664 scopus 로고    scopus 로고
    • Sites for Galpha binding on the G protein beta subunit overlap with sites for regulation of phospholipase Cbeta and adenylyl cyclase
    • Li, Y., Sternweis, P. M., Charnecki, S., Smith, T. F., Gilman, A. G., Neer, E. J., and Kozasa, T. 1998b. Sites for Galpha binding on the G protein beta subunit overlap with sites for regulation of phospholipase Cbeta and adenylyl cyclase. J. Biol. Chem. 273: 16265-72.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16265-16272
    • Li, Y.1    Sternweis, P.M.2    Charnecki, S.3    Smith, T.F.4    Gilman, A.G.5    Neer, E.J.6    Kozasa, T.7
  • 102
    • 0032545277 scopus 로고    scopus 로고
    • Differential activity of the G protein beta5/ gamma2 subunit at receptors and effectors
    • Lindorfer, M. A., Myung, C.-S., Savino, Y., Yasuda, H., Khazan, R. and Garrison, J. C. 1998. Differential activity of the G protein beta5/ gamma2 subunit at receptors and effectors. J. Biol. Chem. 273: 34429-36.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34429-34436
    • Lindorfer, M.A.1    Myung, C.-S.2    Savino, Y.3    Yasuda, H.4    Khazan, R.5    Garrison, J.C.6
  • 103
    • 0033574522 scopus 로고    scopus 로고
    • Interaction of heterotrimeric G protein Galphao with Purkinje cell protein-2. Evidence for a novel nucleotide exchange factor
    • Luo, Y. and Denker, B. M. 1999. Interaction of heterotrimeric G protein Galphao with Purkinje cell protein-2. Evidence for a novel nucleotide exchange factor. J. Biol. Chem. 274: 10685-8.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10685-10688
    • Luo, Y.1    Denker, B.M.2
  • 105
    • 0033515040 scopus 로고    scopus 로고
    • The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit
    • Makino, E. R., Handy, J. W., Li, T., and Arshavsky, V. Y. 1999. The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit. Proc. Natl. Acad. Sci. U.S.A. 96: 1947-52.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1947-1952
    • Makino, E.R.1    Handy, J.W.2    Li, T.3    Arshavsky, V.Y.4
  • 107
    • 0028694342 scopus 로고
    • Activation of Ras by receptor tyrosine kinases
    • Margolis, B., and Skolnik, E. Y. 1994. Activation of Ras by receptor tyrosine kinases. J. Am. Soc. Nephrol. 5: 1288-99.
    • (1994) J. Am. Soc. Nephrol. , vol.5 , pp. 1288-1299
    • Margolis, B.1    Skolnik, E.Y.2
  • 108
    • 0033586724 scopus 로고    scopus 로고
    • Modulation of transducin GTPase activity by chimeric RGS16 and RGS9 regulators of G protein signaling and the effector molecule
    • McEntaffer, R. L., Natochin, M., and Artemyev, N. O. 1999. Modulation of transducin GTPase activity by chimeric RGS16 and RGS9 regulators of G protein signaling and the effector molecule. Biochemistry 38: 4931-7.
    • (1999) Biochemistry , vol.38 , pp. 4931-4937
    • McEntaffer, R.L.1    Natochin, M.2    Artemyev, N.O.3
  • 109
    • 0001793118 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2
    • Mochizuki, N., Cho, G., Wen, B., and Insel, P. A. 1996. Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2. Gene 181: 39-43.
    • (1996) Gene , vol.181 , pp. 39-43
    • Mochizuki, N.1    Cho, G.2    Wen, B.3    Insel, P.A.4
  • 110
  • 112
    • 0030029153 scopus 로고    scopus 로고
    • High affinity binding of beta-adrenergic receptor kinase to microsomal membranes. Modulation of the activity of bound kinase by heterotrimeric G protein activation
    • Murga, C., Ruiz-Gomez, A., Garcia-Higuera, I., Kim, C. M., Benovic, J. L., and Mayor, F., Jr. 1996. High affinity binding of beta-adrenergic receptor kinase to microsomal membranes. Modulation of the activity of bound kinase by heterotrimeric G protein activation. J. Biol. Chem. 271: 985-94.
    • (1996) J. Biol. Chem. , vol.271 , pp. 985-994
    • Murga, C.1    Ruiz-Gomez, A.2    Garcia-Higuera, I.3    Kim, C.M.4    Benovic, J.L.5    Mayor Jr., F.6
  • 113
    • 0025289246 scopus 로고
    • Cell-type-specific early response gene expression during plasmacytoid differentiation of human B lymphocytic leukemia cells
    • Murphy, J. J., and Norton, J. D. 1990. Cell-type-specific early response gene expression during plasmacytoid differentiation of human B lymphocytic leukemia cells. Biochim. Biophys. Acta. 1049: 261-71.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 261-271
    • Murphy, J.J.1    Norton, J.D.2
  • 114
    • 0032992519 scopus 로고    scopus 로고
    • Rhophilin, a small GTPase Rho-binding protein, is abundantly expressed in the mouse testis and localized in the principal piece of the sperm tail
    • Nakamura, K., Fujita, A., Murata, T., Watanabe, G., Mori, C., Fujita, J., Watanabe, N., Ishizaki, T., Yoshida, O., and Narumiya, S. 1999. Rhophilin, a small GTPase Rho-binding protein, is abundantly expressed in the mouse testis and localized in the principal piece of the sperm tail. FEBS Lett. 445: 9-13.
    • (1999) FEBS Lett. , vol.445 , pp. 9-13
    • Nakamura, K.1    Fujita, A.2    Murata, T.3    Watanabe, G.4    Mori, C.5    Fujita, J.6    Watanabe, N.7    Ishizaki, T.8    Yoshida, O.9    Narumiya, S.10
  • 115
    • 0031813650 scopus 로고    scopus 로고
    • Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level
    • Nakamura, T., Hamada, F., Ishidate, T., Anai, K., Kawahara, K., Toyoshima, K., and Akiyama, T. 1998. Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level. Genes Cells 3: 395-403.
    • (1998) Genes Cells , vol.3 , pp. 395-403
    • Nakamura, T.1    Hamada, F.2    Ishidate, T.3    Anai, K.4    Kawahara, K.5    Toyoshima, K.6    Akiyama, T.7
  • 116
    • 0027488049 scopus 로고
    • A B cell specific immediate early human gene is located on chromosome band 1q31 and encodes an alpha helical basic phosphoprotein
    • Newton, J. S., Deed, R. W., Mitchell, E. L. D., Murphy, J. J., and Norton, J. D. 1993. A B cell specific immediate early human gene is located on chromosome band 1q31 and encodes an alpha helical basic phosphoprotein. Biochim. Biophys. Acta. 1216: 314-6.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 314-316
    • Newton, J.S.1    Deed, R.W.2    Mitchell, E.L.D.3    Murphy, J.J.4    Norton, J.D.5
  • 123
    • 0030200001 scopus 로고    scopus 로고
    • Pleckstrin's repeat performance: A novel domain in G-protein signaling?
    • Ponting, C., and Bork, P. 1996. Pleckstrin's repeat performance: a novel domain in G-protein signaling? Trends Biochem. Sci. 21: 245-6.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 245-246
    • Ponting, C.1    Bork, P.2
  • 124
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-membranous sites
    • Ponting, C. P., Phillips, C., Davies, K. E., and Blake, D. J. 1997. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 19: 469-79.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 125
    • 0033564683 scopus 로고    scopus 로고
    • Modulation of the affinity and selectivity of RGS protein interaction with galpha subunits by a conserved Asparagine/Serine residue
    • Posner, B. A., Mukhopadhyay, S., Tesmer, J. J., Gilman, A. G., and Ross, E. M. 1999. Modulation of the affinity and selectivity of RGS protein interaction with galpha subunits by a conserved Asparagine/Serine residue. Biochemistry 38: 7773-9.
    • (1999) Biochemistry , vol.38 , pp. 7773-7779
    • Posner, B.A.1    Mukhopadhyay, S.2    Tesmer, J.J.3    Gilman, A.G.4    Ross, E.M.5
  • 126
    • 0033559843 scopus 로고    scopus 로고
    • Cloning and characterization of RGS9-2: A striatal-enriched alternatively spliced product of the RGS9 gene
    • Rahman, Z., Gold, S. J., Potenza, M. N., Cowan, C. W., Ni, Y. G., He, W., Wensel, T. G., and Nestler, E. J. 1999. Cloning and characterization of RGS9-2: a striatal-enriched alternatively spliced product of the RGS9 gene. J. Neurosci. 19: 2016-26.
    • (1999) J. Neurosci. , vol.19 , pp. 2016-2026
    • Rahman, Z.1    Gold, S.J.2    Potenza, M.N.3    Cowan, C.W.4    Ni, Y.G.5    He, W.6    Wensel, T.G.7    Nestler, E.J.8
  • 127
    • 0031460029 scopus 로고    scopus 로고
    • PDZ domain proteins: Scaffolds for signaling complexes
    • Ranganathan, R. and Ross, E. M. 1997. PDZ domain proteins: scaffolds for signaling complexes. Curr. Biol. 7: R770-3.
    • (1997) Curr. Biol. , vol.7
    • Ranganathan, R.1    Ross, E.M.2
  • 128
    • 0030848936 scopus 로고    scopus 로고
    • Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo
    • Ravichandran, K. S., Zhou, M. M., Pratt, J. C., Harlan, J. E., Walk, S. F., Fesik, S. W., and Burakoff, S. J. 1997. Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo. Mol. Cell. Biol. 17: 5540-9.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5540-5549
    • Ravichandran, K.S.1    Zhou, M.M.2    Pratt, J.C.3    Harlan, J.E.4    Walk, S.F.5    Fesik, S.W.6    Burakoff, S.J.7
  • 129
    • 0025584623 scopus 로고
    • PEST sequences are signals for rapid intracellular proteolysis
    • Rechsteiner, M. 1990. PEST sequences are signals for rapid intracellular proteolysis. Semin. Cell. Biol. 1: 433-40.
    • (1990) Semin. Cell. Biol. , vol.1 , pp. 433-440
    • Rechsteiner, M.1
  • 130
    • 0029867023 scopus 로고    scopus 로고
    • Regulating G Protein Signaling
    • Roush, W. 1996. Regulating G Protein Signaling. Science 271: 1056-8.
    • (1996) Science , vol.271 , pp. 1056-1058
    • Roush, W.1
  • 131
    • 0032539945 scopus 로고
    • Bridging of beta-catenin and glycogen synthase kinase-3beta by Axin and inhibition of beta-catenin-mediated transcription
    • Sakanaka, C., Weiss, J. B., and Williams, L. T. 1988. Bridging of beta-catenin and glycogen synthase kinase-3beta by Axin and inhibition of beta-catenin-mediated transcription. Proc. Natl. Acad. Sci. U.S.A. 95: 3020-3.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3020-3023
    • Sakanaka, C.1    Weiss, J.B.2    Williams, L.T.3
  • 132
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J., and Heldin, C. H. 1996. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21: 455-8.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 133
    • 0031892347 scopus 로고    scopus 로고
    • RGS4 inhibits signaling by group I metabotropic glutamate receptors
    • Saugstad, J. A., Marino, M. J., Folk, J. A., Hepler, J. R., and Conn, P. J. 1998. RGS4 inhibits signaling by group I metabotropic glutamate receptors. J. Neurosci. 18: 905-13.
    • (1998) J. Neurosci. , vol.18 , pp. 905-913
    • Saugstad, J.A.1    Marino, M.J.2    Folk, J.A.3    Hepler, J.R.4    Conn, P.J.5
  • 135
    • 0032575557 scopus 로고    scopus 로고
    • A possible role of RGS9 in phototransduction. A bridge between the cGMP-phosphodiesterase system and the guanylyl cyclase system
    • Seno, K., Kishigami, A., Ihara, S., Maeda, T., Bondarenko, V. A., Nishizawa, Y., Usukura, J., Yamazaki, A., and Hayashi, F. 1998. A possible role of RGS9 in phototransduction. A bridge between the cGMP-phosphodiesterase system and the guanylyl cyclase system. J. Biol Chem. 273: 22169-72.
    • (1998) J. Biol Chem. , vol.273 , pp. 22169-22172
    • Seno, K.1    Kishigami, A.2    Ihara, S.3    Maeda, T.4    Bondarenko, V.A.5    Nishizawa, Y.6    Usukura, J.7    Yamazaki, A.8    Hayashi, F.9
  • 136
    • 0025155076 scopus 로고
    • A set of human putative lymphocyte G0/G1 switch genes includes genes homologous to rodent cytokine and zinc finger protein-encoding genes
    • Siderovski, D. P., Blum, S., Forsdyke, R. E., and Forsdyke, D. R. 1990. A set of human putative lymphocyte G0/G1 switch genes includes genes homologous to rodent cytokine and zinc finger protein-encoding genes. DNA Cell Biol. 9: 579-87.
    • (1990) DNA Cell Biol. , vol.9 , pp. 579-587
    • Siderovski, D.P.1    Blum, S.2    Forsdyke, R.E.3    Forsdyke, D.R.4
  • 137
    • 0030087943 scopus 로고    scopus 로고
    • A new family of regulators of G-protein-coupled receptors?
    • Siderovski, D. P., Hessel, A., Chung, S., Mak, T. W., and Tyers, M. 1996. A new family of regulators of G-protein-coupled receptors? Curr. Biol. 6: 211-2.
    • (1996) Curr. Biol. , vol.6 , pp. 211-212
    • Siderovski, D.P.1    Hessel, A.2    Chung, S.3    Mak, T.W.4    Tyers, M.5
  • 138
    • 0028109139 scopus 로고
    • A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells
    • Siderovski, D. P., Heximer, S. P., and Forsdyke, D. R. 1994. A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells. DNA Cell Biol. 13: 125-47.
    • (1994) DNA Cell Biol. , vol.13 , pp. 125-147
    • Siderovski, D.P.1    Heximer, S.P.2    Forsdyke, D.R.3
  • 140
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I., Strathmann, M. P., and Gautam, N. 1991. Diversity of G proteins in signal transduction. Science 252: 802-808.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 141
    • 0033605581 scopus 로고    scopus 로고
    • The alpha-helical domain of Galphat determines specific interaction with regulator of G protein signaling 9
    • Skiba, N. P., Yang, C. S., Huang, T., Bae, H., and Hamm, H. E. 1999. The alpha-helical domain of Galphat determines specific interaction with regulator of G protein signaling 9. J. Biol. Chem. 274: 8770-8.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8770-8778
    • Skiba, N.P.1    Yang, C.S.2    Huang, T.3    Bae, H.4    Hamm, H.E.5
  • 142
    • 0031456672 scopus 로고    scopus 로고
    • Interaction of Wnt and a Frizzled homologue triggers G-protein-linked phosphatidylinositol signaling
    • Slusarski, D. C., Corces, V. G., and Moon, R. T. 1997. Interaction of Wnt and a Frizzled homologue triggers G-protein-linked phosphatidylinositol signaling. Nature 390: 410-3.
    • (1997) Nature , vol.390 , pp. 410-413
    • Slusarski, D.C.1    Corces, V.G.2    Moon, R.T.3
  • 144
    • 0032509741 scopus 로고    scopus 로고
    • Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/ RGS16): Genomic structure and chromosomal localization of the human gene
    • Snow, B. E., Antonio, L., Suggs, S., and Siderovski, D. P. 1998a. Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/ RGS16): genomic structure and chromosomal localization of the human gene. Gene 206: 247-53.
    • (1998) Gene , vol.206 , pp. 247-253
    • Snow, B.E.1    Antonio, L.2    Suggs, S.3    Siderovski, D.P.4
  • 145
    • 0033038913 scopus 로고    scopus 로고
    • Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11
    • Snow, B. E., Betts, L., Mangion, J., Sondek, J., and Siderovski, D. P. 1999. Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11. Proc. Natl. Acad. Sci. U.S.A. 96: 6489-94.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6489-6494
    • Snow, B.E.1    Betts, L.2    Mangion, J.3    Sondek, J.4    Siderovski, D.P.5
  • 149
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae
    • Broach, J. R., Pringle, J. R., and Jones, E. W., Eds., Cold Spring Harbor Laboratory Press, New York
    • Sprague, G. F., Jr. and Thorner, J. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae. In: The Molecular and Cellular Biology of the Yeast Saccharomyces. Broach, J. R., Pringle, J. R., and Jones, E. W., Eds., Cold Spring Harbor Laboratory Press, New York, 657-744.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces , pp. 657-744
    • Sprague Jr., G.F.1    Thorner, J.2
  • 150
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4-activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis
    • Tesmer, J. J., Berman, D. M., Gilman, A. G., and Sprang, S. R. 1997. Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell 89: 251-61.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 151
    • 0032053616 scopus 로고    scopus 로고
    • RGS9: A regulator of G-protein signalling with specific expression in rat and mouse striatum
    • Thomas, E. A., Danielson, P. E., and Sutcliffe, J. G. 1998. RGS9: a regulator of G-protein signalling with specific expression in rat and mouse striatum. J. Neurosci. Res. 52: 118-24.
    • (1998) J. Neurosci. Res. , vol.52 , pp. 118-124
    • Thomas, E.A.1    Danielson, P.E.2    Sutcliffe, J.G.3
  • 152
    • 0028891875 scopus 로고
    • Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4,5-bisphosphate binding
    • Touhara, K., Koch, W. J., Hawes, B. E., and Lefkowitz, R. J. 1995. Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4,5-bisphosphate binding. J. Biol. Chem. 270: 17000-5.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17000-17005
    • Touhara, K.1    Koch, W.J.2    Hawes, B.E.3    Lefkowitz, R.J.4
  • 153
    • 0031767445 scopus 로고    scopus 로고
    • Role of regulator of G protein signaling in desensitization of the glucose-dependent insulinotropic peptide receptor
    • Tseng, C.-C. and Zhang, X.-Y. 1998. Role of regulator of G protein signaling in desensitization of the glucose-dependent insulinotropic peptide receptor. Endocrinology 139: 4470-5.
    • (1998) Endocrinology , vol.139 , pp. 4470-4475
    • Tseng, C.-C.1    Zhang, X.-Y.2
  • 155
    • 0030776825 scopus 로고    scopus 로고
    • Two dominant mutations in the mouse fused gene are the result of transposon insertions
    • Vasicek, T. J., Zeng, L., Guan, X. J., Zhang, T., Costantini, F., and Tilghman, S. M. 1997. Two dominant mutations in the mouse fused gene are the result of transposon insertions. Genetics 147: 777-86.
    • (1997) Genetics , vol.147 , pp. 777-786
    • Vasicek, T.J.1    Zeng, L.2    Guan, X.J.3    Zhang, T.4    Costantini, F.5    Tilghman, S.M.6
  • 157
    • 0032530652 scopus 로고    scopus 로고
    • Structural basis of activity and subunit recognition in G protein heterotrimers
    • Wall, M. A., Posner, B.A., and Sprang, S. R. 1998. Structural basis of activity and subunit recognition in G protein heterotrimers. Structure 6: 1169-1183.
    • (1998) Structure , vol.6 , pp. 1169-1183
    • Wall, M.A.1    Posner, B.A.2    Sprang, S.R.3
  • 159
    • 0029985041 scopus 로고    scopus 로고
    • A novel form of the G protein beta subunit Gbeta5 is specifically expressed in the vertebrate retina
    • Watson, A. J., Aragay, A. M., Slepak, V. Z., and Simon, M. I. 1996a. A novel form of the G protein beta subunit Gbeta5 is specifically expressed in the vertebrate retina. J. Biol. Chem. 271: 28154-60.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28154-28160
    • Watson, A.J.1    Aragay, A.M.2    Slepak, V.Z.3    Simon, M.I.4
  • 160
    • 0028068380 scopus 로고
    • A fifth member of the mammalian G-protein beta-subunit family. Expression in brain and activation of the beta 2 isotype of phospholipase C
    • Watson, A. J., Katz, A., and Simon, M. I. 1994. A fifth member of the mammalian G-protein beta-subunit family. Expression in brain and activation of the beta 2 isotype of phospholipase C. J. Biol. Chem. 269: 22150-6.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22150-22156
    • Watson, A.J.1    Katz, A.2    Simon, M.I.3
  • 161
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits
    • Watson, N., Linder, M. E., Druey, K. M., Kehrl, J. H., and Blumer, K. J. 1996b. RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Nature 383: 172-5.
    • (1996) Nature , vol.383 , pp. 172-175
    • Watson, N.1    Linder, M.E.2    Druey, K.M.3    Kehrl, J.H.4    Blumer, K.J.5
  • 163
    • 0028295681 scopus 로고
    • The C. elegans genome project: Contiguous nucleotide sequence of over two megabases from chromosome III
    • Wilson, R. et al. 1994. The C. elegans genome project: contiguous nucleotide sequence of over two megabases from chromosome III. Nature 368: 32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 165
    • 0029115312 scopus 로고
    • Differential expression of a basic helix-loop-helix phosphoprotein gene, G0S8, in acute leukemia and localization to human chromosome 1q31
    • Wu, H. K., Heng, H. H., Shi, X. M., Forsdyke, D. R., Tsui, L. C., Mak, T. W., Minden, M. D., and Siderovski, D. P. 1995. Differential expression of a basic helix-loop-helix phosphoprotein gene, G0S8, in acute leukemia and localization to human chromosome 1q31. Leukemia 9: 1291-8.
    • (1995) Leukemia , vol.9 , pp. 1291-1298
    • Wu, H.K.1    Heng, H.H.2    Shi, X.M.3    Forsdyke, D.R.4    Tsui, L.C.5    Mak, T.W.6    Minden, M.D.7    Siderovski, D.P.8
  • 167
    • 0029019969 scopus 로고
    • Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila-disabled gene product
    • Xu, X. X., Yang, W., Jackowski, S., and Rock, C. O. 1995. Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila-disabled gene product. J. Biol. Chem. 270: 14184-91.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14184-14191
    • Xu, X.X.1    Yang, W.2    Jackowski, S.3    Rock, C.O.4
  • 168
    • 0032568219 scopus 로고    scopus 로고
    • Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2
    • Xu, X. X., Yi, T., Tang, B., and Lambeth, J. D. 1998. Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2. Oncogene 16: 1561-9.
    • (1998) Oncogene , vol.16 , pp. 1561-1569
    • Xu, X.X.1    Yi, T.2    Tang, B.3    Lambeth, J.D.4
  • 169
    • 0031943002 scopus 로고    scopus 로고
    • Axil, a member of the axin family, interacts with both glycogen synthase kinase 3-beta and beta-catenin and inhibits axis formation of Xenopus embryos
    • Yamamoto, H., Kishida, S., Uochi, T., Ikeda, S., Koyama, S., Asashima, M., and Kikuchi, A. 1998. Axil, a member of the axin family, interacts with both glycogen synthase kinase 3-beta and beta-catenin and inhibits axis formation of Xenopus embryos. Mol. Cell. Biol. 18: 2867-75.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2867-2875
    • Yamamoto, H.1    Kishida, S.2    Uochi, T.3    Ikeda, S.4    Koyama, S.5    Asashima, M.6    Kikuchi, A.7
  • 172
    • 0030468336 scopus 로고    scopus 로고
    • Selective activation of effector pathways by brain-specific G protein beta5
    • Zhang, S., Coso, O. A., Lee, C., Gutkind, J. S., and Simonds, W. F. 1996. Selective activation of effector pathways by brain-specific G protein beta5. J. Biol. Chem. 271: 33575-9.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33575-33579
    • Zhang, S.1    Coso, O.A.2    Lee, C.3    Gutkind, J.S.4    Simonds, W.F.5
  • 173
    • 0033613580 scopus 로고    scopus 로고
    • RGS16 attenuates galphaq-dependent p38 mitogen-activated protein kinase activation by platelet-activating factor
    • Zhang, Y., Neo, S. Y., Han, J., Yaw, L. P., and Lin, S. C. 1999. RGS16 attenuates galphaq-dependent p38 mitogen-activated protein kinase activation by platelet-activating factor. J. Biol. Chem. 274: 2851-7.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2851-2857
    • Zhang, Y.1    Neo, S.Y.2    Han, J.3    Yaw, L.P.4    Lin, S.C.5
  • 174
    • 0030723614 scopus 로고    scopus 로고
    • Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain
    • Zhang, Z., Lee, C. H., Mandiyan, V., Borg, J. P., Margolis, B., Schlessinger, J., and Kuriyan, J. 1997. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J. 16: 6141-50.
    • (1997) EMBO J. , vol.16 , pp. 6141-6150
    • Zhang, Z.1    Lee, C.H.2    Mandiyan, V.3    Borg, J.P.4    Margolis, B.5    Schlessinger, J.6    Kuriyan, J.7
  • 175
    • 0029010308 scopus 로고
    • The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif
    • Zhou, S., Margolis, B., Chaudhuri, M., Shoelson, S. E., and Cantley, L. C. 1995. The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif. J. Biol. Chem. 270: 14863-6.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14863-14866
    • Zhou, S.1    Margolis, B.2    Chaudhuri, M.3    Shoelson, S.E.4    Cantley, L.C.5
  • 176
    • 0032541613 scopus 로고    scopus 로고
    • Rho family proteins and Ras transformation: The RHOad less traveled gets congested
    • Zohn, I. M., Campbell, S. L., Khosravi-Far, R., Rossman, K. L., and Der, C. J. 1998. Rho family proteins and Ras transformation: the RHOad less traveled gets congested. Oncogene 17: 1415-38.
    • (1998) Oncogene , vol.17 , pp. 1415-1438
    • Zohn, I.M.1    Campbell, S.L.2    Khosravi-Far, R.3    Rossman, K.L.4    Der, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.