메뉴 건너뛰기




Volumn 65, Issue , 2004, Pages 189-210

G-Protein Coupled Receptors and Calcium Signaling in Development

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; CELL SURFACE RECEPTOR; G PROTEIN COUPLED RECEPTOR; PROTEIN SUBUNIT;

EID: 15544386243     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2153(04)65007-1     Document Type: Article
Times cited : (2)

References (125)
  • 1
    • 2242453282 scopus 로고    scopus 로고
    • Signaling of rat frizzled-2 through phosphodiesterase and cyclic GMP
    • Ahumada A., Slusarski D.C., Liu X., Moon R.T., Malbon C.C., and Wang H. Signaling of rat frizzled-2 through phosphodiesterase and cyclic GMP. Science 298 (2002) 2006-2010
    • (2002) Science , vol.298 , pp. 2006-2010
    • Ahumada, A.1    Slusarski, D.C.2    Liu, X.3    Moon, R.T.4    Malbon, C.C.5    Wang, H.6
  • 3
    • 0030059443 scopus 로고    scopus 로고
    • Modulation of Xenopus embryo mesoderm-specific gene expression and dorsoanterior patterning by receptors that activate the phosphatidylinositol cycle signal transduction pathway
    • Ault K.T., Durmowicz G., Galione A., Harger P.L., and Busa W.B. Modulation of Xenopus embryo mesoderm-specific gene expression and dorsoanterior patterning by receptors that activate the phosphatidylinositol cycle signal transduction pathway. Development 122 (1996) 2033-2041
    • (1996) Development , vol.122 , pp. 2033-2041
    • Ault, K.T.1    Durmowicz, G.2    Galione, A.3    Harger, P.L.4    Busa, W.B.5
  • 5
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennett Jr. W.S., and Steitz T.A. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. USA 75 (1978) 4848-4852
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4848-4852
    • Bennett Jr., W.S.1    Steitz, T.A.2
  • 6
    • 0026722913 scopus 로고
    • Reconstitution of agonist-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis using purified m1 muscarinic receptor, Gq{plus 45 degree rule}11, and phospholipase C-beta 1
    • Berstein G., Blank J.L., Smrcka A.V., Higashijima T., Sternweis P.C., Exton J.H., and Ross E.M. Reconstitution of agonist-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis using purified m1 muscarinic receptor, Gq{plus 45 degree rule}11, and phospholipase C-beta 1. J. Biol. Chem. 267 (1992) 8081-8088
    • (1992) J. Biol. Chem. , vol.267 , pp. 8081-8088
    • Berstein, G.1    Blank, J.L.2    Smrcka, A.V.3    Higashijima, T.4    Sternweis, P.C.5    Exton, J.H.6    Ross, E.M.7
  • 7
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge M.J. Capacitative calcium entry. Biochem. J. 312 (1995) 1-11
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 8
    • 0004479725 scopus 로고    scopus 로고
    • Calcium signaling
    • Heldin C.-H., and Thornes Purton M.S. (Eds), Chestenham
    • Berridge M.J., and Bootman M.D. Calcium signaling. In: Heldin C.-H., and Thornes Purton M.S. (Eds). "Signal Transduction" (1996), Chestenham 205-223
    • (1996) "Signal Transduction" , pp. 205-223
    • Berridge, M.J.1    Bootman, M.D.2
  • 9
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • Berridge M.J., Lipp P., and Bootman M.D. The versatility and universality of calcium signalling. Nat. Rev. 1 (2000) 11-21
    • (2000) Nat. Rev. , vol.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 10
    • 0032801648 scopus 로고    scopus 로고
    • Sodium{plus 45 degree rule}calcium exchange: Its physiological implications
    • Blaustein M.P., and Lederer W.J. Sodium{plus 45 degree rule}calcium exchange: Its physiological implications. Physiol. Rev. 79 (1999) 763-854
    • (1999) Physiol. Rev. , vol.79 , pp. 763-854
    • Blaustein, M.P.1    Lederer, W.J.2
  • 11
    • 0033518295 scopus 로고    scopus 로고
    • Calcium signalling: Ringing changes to the "bell-shaped curve"
    • Bootman M.D., and Lipp P. Calcium signalling: Ringing changes to the "bell-shaped curve". Curr. Biol. 9 (1999) 876-878
    • (1999) Curr. Biol. , vol.9 , pp. 876-878
    • Bootman, M.D.1    Lipp, P.2
  • 13
    • 0041534404 scopus 로고    scopus 로고
    • 2+ signalling in mitochondria: Mechanism and role in physiology and pathology
    • 2+ signalling in mitochondria: Mechanism and role in physiology and pathology. Cell Calcium 34 (2003) 399-405
    • (2003) Cell Calcium , vol.34 , pp. 399-405
    • Brini, M.1
  • 15
    • 0344780741 scopus 로고    scopus 로고
    • G-protein coupled receptor kinases as modulators of G-protein signalling
    • Bünemann M., and Hosey M.M. G-protein coupled receptor kinases as modulators of G-protein signalling. J. Physiol. 517 (1999) 5-23
    • (1999) J. Physiol. , vol.517 , pp. 5-23
    • Bünemann, M.1    Hosey, M.M.2
  • 16
    • 0032966473 scopus 로고    scopus 로고
    • Gene regulation by patterned electrical activity during neural and skeletal muscle development
    • Buonanno A., and Fields R.D. Gene regulation by patterned electrical activity during neural and skeletal muscle development. Curr. Opin. Neurobiol. 9 (1999) 110-120
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 110-120
    • Buonanno, A.1    Fields, R.D.2
  • 17
    • 1242339614 scopus 로고    scopus 로고
    • Molecular cloning of a sixth member of the K+-dependent Na+{plus 45 degree rule}Ca2+ exchanger gene family, NCKX6
    • Cai X., and Lytton J. Molecular cloning of a sixth member of the K+-dependent Na+{plus 45 degree rule}Ca2+ exchanger gene family, NCKX6. J. Biol. Chem. 279 (2004) 5867-5876
    • (2004) J. Biol. Chem. , vol.279 , pp. 5867-5876
    • Cai, X.1    Lytton, J.2
  • 20
    • 0033522228 scopus 로고    scopus 로고
    • 2+-signalling patterns by NAADP in pancreatic acinar cells
    • 2+-signalling patterns by NAADP in pancreatic acinar cells. Nature 398 (1999) 74-76
    • (1999) Nature , vol.398 , pp. 74-76
    • Cancela, J.M.1    Churchill, G.C.2    Galione, A.3
  • 21
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli E. Calcium pump of the plasma membrane. Physiol. Rev. 71 (1992) 283-292
    • (1992) Physiol. Rev. , vol.71 , pp. 283-292
    • Carafoli, E.1
  • 22
    • 0028984532 scopus 로고
    • 2+ stores in platelets, as identified by their differential sensitivity to 2,5-di-(tert-butyl)-1,4-benzohydroquinone and thapsigargin
    • 2+ stores in platelets, as identified by their differential sensitivity to 2,5-di-(tert-butyl)-1,4-benzohydroquinone and thapsigargin. Biochem. J. 310 (1995) 449-452
    • (1995) Biochem. J. , vol.310 , pp. 449-452
    • Cavallini, L.1    Coassin, M.2    Alexandre, A.3
  • 24
    • 0032497843 scopus 로고    scopus 로고
    • Bridging the GAP in inositol 1,3,4,5-tetrakisphosphate signalling
    • Cullen P.J. Bridging the GAP in inositol 1,3,4,5-tetrakisphosphate signalling. Biochim. Biophys. Acta 1436 (1998) 35-47
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 35-47
    • Cullen, P.J.1
  • 25
    • 0036244913 scopus 로고    scopus 로고
    • The Frizzled-1{plus 45 degree rule}beta2-adrenergic receptor chimera: Pharmacological properties of a unique G protein-linked receptor
    • DeCostanzo A.J., Huang X.-P., Wang H., and Malbon C.C. The Frizzled-1{plus 45 degree rule}beta2-adrenergic receptor chimera: Pharmacological properties of a unique G protein-linked receptor. Naunyn-Schmiedeberg's Arch. Pharmacol. 365 (2002) 341-348
    • (2002) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.365 , pp. 341-348
    • DeCostanzo, A.J.1    Huang, X.-P.2    Wang, H.3    Malbon, C.C.4
  • 26
    • 0021269910 scopus 로고
    • Synergistic effect of A23187 and a phorbol ester on amylase secretion from rabbit pancreatic acini
    • De Pont J.J.H.H., and Fleuren-Jakobs A.M.M. Synergistic effect of A23187 and a phorbol ester on amylase secretion from rabbit pancreatic acini. FEBS Lett. 170 (1984) 64-68
    • (1984) FEBS Lett. , vol.170 , pp. 64-68
    • De Pont, J.J.H.H.1    Fleuren-Jakobs, A.M.M.2
  • 27
    • 0028896146 scopus 로고
    • Involvement of ryanodine receptors in sphingosylphosphorylcholine-induced calcium release from brain microsomes
    • Dettbarn C., Betto R., Salviati G., Sabbadini R., and Palade P. Involvement of ryanodine receptors in sphingosylphosphorylcholine-induced calcium release from brain microsomes. Brain Res. 669 (1995) 79-85
    • (1995) Brain Res. , vol.669 , pp. 79-85
    • Dettbarn, C.1    Betto, R.2    Salviati, G.3    Sabbadini, R.4    Palade, P.5
  • 30
    • 0030948743 scopus 로고    scopus 로고
    • New developments in phospholipase D
    • Exton J.H. New developments in phospholipase D. J. Biol. Chem. 272 (1997) 15579-15582
    • (1997) J. Biol. Chem. , vol.272 , pp. 15579-15582
    • Exton, J.H.1
  • 31
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Farahbakhsh Z.T., Hideg K., and Hubbell W.L. Photoactivated conformational changes in rhodopsin: A time-resolved spin label study. Science 262 (1993) 1416-1419
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 32
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson S.S. Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling. Pharmacol. Rev. 53 (2001) 1-24
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 33
    • 0023784091 scopus 로고
    • Ryanodine receptor channel of sarcoplasmic reticulum
    • Fill M., and Coronado R. Ryanodine receptor channel of sarcoplasmic reticulum. Trends Neurosci. 11 (1988) 453-457
    • (1988) Trends Neurosci. , vol.11 , pp. 453-457
    • Fill, M.1    Coronado, R.2
  • 34
    • 0028128083 scopus 로고
    • Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signalling
    • Galione A. Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signalling. Mol. Cell. Endocrinol. 98 (1994) 125-131
    • (1994) Mol. Cell. Endocrinol. , vol.98 , pp. 125-131
    • Galione, A.1
  • 35
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II. Mechanism of agonist activation
    • Gether U., and Kobilka B.K. G protein-coupled receptors. II. Mechanism of agonist activation. J. Biol. Chem. 273 (1998) 17979-17982
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 36
    • 0028856707 scopus 로고
    • 2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • 2 adrenergic receptor. Evidence for ligand-specific conformational changes. J. Biol. Chem. 270 (1995) 28268-28275
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 37
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gillman A.G. G proteins: Transducers of receptor-generated signals. Annu. Rev. Biochem. 56 (1987) 615-649
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gillman, A.G.1
  • 38
    • 0035730136 scopus 로고    scopus 로고
    • Participation of mitochondria in calcium signalling in the exocrine pancreas
    • Gonzalez A., and Salido G.M. Participation of mitochondria in calcium signalling in the exocrine pancreas. J. Physiol. Biochem. 57 (2001) 331-339
    • (2001) J. Physiol. Biochem. , vol.57 , pp. 331-339
    • Gonzalez, A.1    Salido, G.M.2
  • 39
    • 0031961103 scopus 로고    scopus 로고
    • The significance of the isoforms of plasma membrane calcium ATPase
    • Guerini D. The significance of the isoforms of plasma membrane calcium ATPase. Cell Tissue Res. 292 (1998) 191-197
    • (1998) Cell Tissue Res. , vol.292 , pp. 191-197
    • Guerini, D.1
  • 40
    • 0037439138 scopus 로고    scopus 로고
    • Coactivation of Rac and Rho by Wnt{plus 45 degree rule}Frizzled signaling is required for vertebrate gastrulation
    • Habas R., Dawid I.B., and He X. Coactivation of Rac and Rho by Wnt{plus 45 degree rule}Frizzled signaling is required for vertebrate gastrulation. Genes Dev. 17 (2003) 295-309
    • (2003) Genes Dev. , vol.17 , pp. 295-309
    • Habas, R.1    Dawid, I.B.2    He, X.3
  • 41
    • 0346732272 scopus 로고    scopus 로고
    • Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium
    • Hamada K., Terauchi A., and Mikoshiba K. Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium. J. Biol. Chem. 278 (2003) 52881-52889
    • (2003) J. Biol. Chem. , vol.278 , pp. 52881-52889
    • Hamada, K.1    Terauchi, A.2    Mikoshiba, K.3
  • 42
    • 0031263887 scopus 로고    scopus 로고
    • Development of calcium signalling mechanisms during maturation of human oocytes
    • Herbert M., Gillespie J.I., and Murdoch A.P. Development of calcium signalling mechanisms during maturation of human oocytes. Mol. Hum. Reprod. 3 (1997) 965-973
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 965-973
    • Herbert, M.1    Gillespie, J.I.2    Murdoch, A.P.3
  • 43
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas F., Jouaville L.S., and Mazat J.P. Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell 89 (1997) 1145-1153
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 44
    • 0025195367 scopus 로고
    • 2+ entry by inositol phosphates-A possible mechanism
    • 2+ entry by inositol phosphates-A possible mechanism. FEBS Lett. 263 (1990) 5-9
    • (1990) FEBS Lett. , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 45
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. I. Diversity of receptor-ligand interactions
    • Ji T.H., Grossmann M., and Ji I. G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273 (1998) 17299-17302
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 46
    • 0028861715 scopus 로고
    • Activation membrane-receptors
    • Ji T.H., Murdoch W.J., and Ji I. Activation membrane-receptors. Endocrine 3 (1995) 187-194
    • (1995) Endocrine , vol.3 , pp. 187-194
    • Ji, T.H.1    Murdoch, W.J.2    Ji, I.3
  • 47
    • 0034734605 scopus 로고    scopus 로고
    • The mechanism of phospholipase C-gamma1 regulation
    • Kim M.J., Kim E., Ryu S.H., and Suh P.G. The mechanism of phospholipase C-gamma1 regulation. Exp. Mol. Med. 32 (2000) 101-109
    • (2000) Exp. Mol. Med. , vol.32 , pp. 101-109
    • Kim, M.J.1    Kim, E.2    Ryu, S.H.3    Suh, P.G.4
  • 49
    • 0026752495 scopus 로고
    • Different beta-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss C., Scherubl H., Hescheler J., Schultz G., and Wittig B. Different beta-subunits determine G-protein interaction with transmembrane receptors. Nature 358 (1992) 424-426
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 50
    • 0014235891 scopus 로고
    • The catalytic and regulatory properties of enzymes
    • Koshland Jr. D.E., and Neet K.E. The catalytic and regulatory properties of enzymes. Annu. Rev. Biochem. 37 (1968) 359-410
    • (1968) Annu. Rev. Biochem. , vol.37 , pp. 359-410
    • Koshland Jr., D.E.1    Neet, K.E.2
  • 51
    • 3843127850 scopus 로고    scopus 로고
    • Kühl M. (Ed), Landes Biosiences and Kluwer Academic{plus 45 degree rule}Plenum Publishers, Georgetown, TX
    • In: Kühl M. (Ed). "Wnt Signaling in Development." (2003), Landes Biosiences and Kluwer Academic{plus 45 degree rule}Plenum Publishers, Georgetown, TX
    • (2003) "Wnt Signaling in Development."
  • 53
    • 0343293801 scopus 로고    scopus 로고
    • Ca2+{plus 45 degree rule}calmodulin-dependent protein kinase II is stimulated by Wnt and Frizzled homologs and promotes ventral cell fates in Xenopus
    • Kühl M., Sheldahl L.C., Malbon C.C., and Moon R.T. Ca2+{plus 45 degree rule}calmodulin-dependent protein kinase II is stimulated by Wnt and Frizzled homologs and promotes ventral cell fates in Xenopus. J. Biol. Chem. 275 (2000) 12701-12711
    • (2000) J. Biol. Chem. , vol.275 , pp. 12701-12711
    • Kühl, M.1    Sheldahl, L.C.2    Malbon, C.C.3    Moon, R.T.4
  • 55
    • 0028950282 scopus 로고
    • A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose
    • Lee H.C., and Aarhus R. A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose. J. Biol. Chem. 270 (1995) 2152-2157
    • (1995) J. Biol. Chem. , vol.270 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 56
    • 0032563291 scopus 로고    scopus 로고
    • G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization
    • Lefkowitz R.J. G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. J. Biol. Chem. 273 (1998) 18677-18680
    • (1998) J. Biol. Chem. , vol.273 , pp. 18677-18680
    • Lefkowitz, R.J.1
  • 58
    • 0035216832 scopus 로고    scopus 로고
    • Mitochondrial modulation of calcium signaling at the initiation of development
    • Liu L., Hammar K., Smith P.J., Inoue S., and Keefe D.L. Mitochondrial modulation of calcium signaling at the initiation of development. Cell Calcium 30 (2001) 423-433
    • (2001) Cell Calcium , vol.30 , pp. 423-433
    • Liu, L.1    Hammar, K.2    Smith, P.J.3    Inoue, S.4    Keefe, D.L.5
  • 59
    • 0033405618 scopus 로고    scopus 로고
    • Activation of a Frizzled-2{plus 45 degree rule}beta-adrenergic receptor chimera promotes Wnt signaling and differentiation of mouse F9 teratocarcinoma cells via Galphao and Galphat
    • Liu X., Liu T., Slusarski D.C., Yang-Snyder J., Malbon C.C., Moon R.T., and Wang H. Activation of a Frizzled-2{plus 45 degree rule}beta-adrenergic receptor chimera promotes Wnt signaling and differentiation of mouse F9 teratocarcinoma cells via Galphao and Galphat. Proc. Natl. Acad. Sci. USA 96 (1999) 14383-14388
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14383-14388
    • Liu, X.1    Liu, T.2    Slusarski, D.C.3    Yang-Snyder, J.4    Malbon, C.C.5    Moon, R.T.6    Wang, H.7
  • 61
    • 0026442534 scopus 로고
    • Do G protein subunits associate via a three-stranded coiled coil?
    • Lupas A.N., Lupas J.M., and Stock J.B. Do G protein subunits associate via a three-stranded coiled coil?. FEBS Lett. 314 (1992) 105-108
    • (1992) FEBS Lett. , vol.314 , pp. 105-108
    • Lupas, A.N.1    Lupas, J.M.2    Stock, J.B.3
  • 65
    • 0028301325 scopus 로고
    • Calcium channels: Cellular roles and molecular mechanisms
    • McCleskey E.W. Calcium channels: Cellular roles and molecular mechanisms. Curr. Opinion Neurobiol. 4 (1994) 304-312
    • (1994) Curr. Opinion Neurobiol. , vol.4 , pp. 304-312
    • McCleskey, E.W.1
  • 66
    • 0027335760 scopus 로고
    • The ryanodine receptor{plus 45 degree rule}Ca2+ release channel
    • McPherson P.S., and Campbell K.P. The ryanodine receptor{plus 45 degree rule}Ca2+ release channel. J. Biol. Chem. 268 (1993) 13765-13768
    • (1993) J. Biol. Chem. , vol.268 , pp. 13765-13768
    • McPherson, P.S.1    Campbell, K.P.2
  • 67
    • 0028232968 scopus 로고
    • Calcium, calmodulin, and cell cycle regulation
    • Means A.R. Calcium, calmodulin, and cell cycle regulation. FEBS Lett. 347 (1994) 1-4
    • (1994) FEBS Lett. , vol.347 , pp. 1-4
    • Means, A.R.1
  • 68
    • 0027512040 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor
    • Mikoshiba K. Inositol 1,4,5-trisphosphate receptor. Trends. Pharmacol. Sci. 14 (1993) 86-89
    • (1993) Trends. Pharmacol. Sci. , vol.14 , pp. 86-89
    • Mikoshiba, K.1
  • 70
    • 0033565230 scopus 로고    scopus 로고
    • Calcium binding capacity of the cytosol and endoplasmic reticulum of mouse pancreatic acinar cells
    • Mogami H., Gardner J., Gerasimenko O.V., Camello P., Petersen O.H., and Tepikin A.V. Calcium binding capacity of the cytosol and endoplasmic reticulum of mouse pancreatic acinar cells. J. Physiol. 518 (1999) 463-467
    • (1999) J. Physiol. , vol.518 , pp. 463-467
    • Mogami, H.1    Gardner, J.2    Gerasimenko, O.V.3    Camello, P.4    Petersen, O.H.5    Tepikin, A.V.6
  • 72
    • 0033407065 scopus 로고    scopus 로고
    • 2+ signaling complexes in polarized cells
    • 2+ signaling complexes in polarized cells. Cell Calcium 26 (1999) 173-180
    • (1999) Cell Calcium , vol.26 , pp. 173-180
    • Muallem, S.1    Wilkie, T.M.2
  • 74
    • 0020524517 scopus 로고
    • Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin
    • Nathan J., and Hogness D.S. Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell 34 (1983) 807-814
    • (1983) Cell , vol.34 , pp. 807-814
    • Nathan, J.1    Hogness, D.S.2
  • 76
    • 0026649940 scopus 로고
    • Calcium gradients and buffers in bovine chromaffin cells
    • Neher E., and Augustine G.J. Calcium gradients and buffers in bovine chromaffin cells. J. Physiol. 450 (1992) 273-301
    • (1992) J. Physiol. , vol.450 , pp. 273-301
    • Neher, E.1    Augustine, G.J.2
  • 79
    • 0037043688 scopus 로고    scopus 로고
    • Wnt-11 activation of a non-canonical Wnt signaling pathway is required for cardiogenesis
    • Pandur P., Läsche M., Eisenberg L.M., and Kühl M. Wnt-11 activation of a non-canonical Wnt signaling pathway is required for cardiogenesis. Nature 418 (2002) 636-641
    • (2002) Nature , vol.418 , pp. 636-641
    • Pandur, P.1    Läsche, M.2    Eisenberg, L.M.3    Kühl, M.4
  • 80
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh A.B., and Penner R. Store depletion and calcium influx. Physiol. Rev. 77 (1997) 901-930
    • (1997) Physiol. Rev. , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 81
    • 0033168582 scopus 로고    scopus 로고
    • Oxidizing effects of vanadate on calcium mobilization and amylase release in rat pancreatic acinar cells
    • Pariente J.A., Lajas A.I., Pozo M.J., Camello P.J., and Salido G.M. Oxidizing effects of vanadate on calcium mobilization and amylase release in rat pancreatic acinar cells. Biochem. Pharmacol. 58 (1999) 77-84
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 77-84
    • Pariente, J.A.1    Lajas, A.I.2    Pozo, M.J.3    Camello, P.J.4    Salido, G.M.5
  • 82
    • 0035142953 scopus 로고    scopus 로고
    • Release of calcium from mitochondrial and nonmitochondrial intracellular stores in mouse pancreatic acinar cells by hydrogen peroxide
    • Pariente J.A., Camello C., Camello P.J., and Salido G.M. Release of calcium from mitochondrial and nonmitochondrial intracellular stores in mouse pancreatic acinar cells by hydrogen peroxide. J. Membr. Biol. 179 (2001) 27-35
    • (2001) J. Membr. Biol. , vol.179 , pp. 27-35
    • Pariente, J.A.1    Camello, C.2    Camello, P.J.3    Salido, G.M.4
  • 84
    • 1242321159 scopus 로고    scopus 로고
    • 2+ release-A new signalling pathway
    • 2+ release-A new signalling pathway. Biol. Cell 96 (2004) 19-28
    • (2004) Biol. Cell , vol.96 , pp. 19-28
    • Patel, S.1
  • 86
    • 33646830005 scopus 로고
    • Ion motive ATPase. I. Ubiquity, properties, and significance for cell function
    • Pedersen P.L., and Carafoli E. Ion motive ATPase. I. Ubiquity, properties, and significance for cell function. Trends Biochem. Sci. 12 (1987) 146-150
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 88
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., and Pentyala S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80 (2000) 1291-1335
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 89
    • 0026634314 scopus 로고
    • Regulation of contraction and relaxation in arterial smooth muscle
    • Reembold C.M. Regulation of contraction and relaxation in arterial smooth muscle. Hypertension 20 (1992) 129-137
    • (1992) Hypertension , vol.20 , pp. 129-137
    • Reembold, C.M.1
  • 91
    • 0032540370 scopus 로고    scopus 로고
    • Morphological consequences of altered calcium-dependent transmembrane signaling on the development of cultured cerebellar Purkinje neurons
    • Reitstetter R., and Yool A.J. Morphological consequences of altered calcium-dependent transmembrane signaling on the development of cultured cerebellar Purkinje neurons. Brain. Res. Dev. Brain Res. 107 (1998) 165-167
    • (1998) Brain. Res. Dev. Brain Res. , vol.107 , pp. 165-167
    • Reitstetter, R.1    Yool, A.J.2
  • 92
    • 0018851861 scopus 로고
    • The role of hormone receptors and GTP-regulatory proteins in membrane transduction
    • Rodbell M. The role of hormone receptors and GTP-regulatory proteins in membrane transduction. Nature 284 (1980) 17-22
    • (1980) Nature , vol.284 , pp. 17-22
    • Rodbell, M.1
  • 94
    • 0034677783 scopus 로고    scopus 로고
    • A role for the actin cytoskeleton in the initiation and maintenance of store-mediated calcium entry in human platelets. Evidence for conformational coupling
    • Rosado J.A., Jenner S., and Sage S.O. A role for the actin cytoskeleton in the initiation and maintenance of store-mediated calcium entry in human platelets. Evidence for conformational coupling. J. Biol. Chem. 275 (2000) 7527-7533
    • (2000) J. Biol. Chem. , vol.275 , pp. 7527-7533
    • Rosado, J.A.1    Jenner, S.2    Sage, S.O.3
  • 95
    • 0034667659 scopus 로고    scopus 로고
    • 2+ entry in human platelets through the reorganization of the actin cytoskeleton
    • 2+ entry in human platelets through the reorganization of the actin cytoskeleton. Biochem. J. 351 (2000) 429-437
    • (2000) Biochem. J. , vol.351 , pp. 429-437
    • Rosado, J.A.1    Graves, D.2    Sage, S.O.3
  • 96
    • 0034176274 scopus 로고    scopus 로고
    • 2+ entry in human platelets: Evidence for involvement of small GTP-binding proteins and actin cytoskeleton
    • 2+ entry in human platelets: Evidence for involvement of small GTP-binding proteins and actin cytoskeleton. Biochem. J. 347 (2000) 183-192
    • (2000) Biochem. J. , vol.347 , pp. 183-192
    • Rosado, J.A.1    Sage, S.O.2
  • 97
    • 0034733604 scopus 로고    scopus 로고
    • 2+-ATPase by small GTPases and phosphoinositides in human platelets
    • 2+-ATPase by small GTPases and phosphoinositides in human platelets. J. Biol. Chem. 275 (2000) 19529-19535
    • (2000) J. Biol. Chem. , vol.275 , pp. 19529-19535
    • Rosado, J.A.1    Sage, S.O.2
  • 99
  • 101
    • 0037118064 scopus 로고    scopus 로고
    • The Wnt{plus 45 degree rule}calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos
    • Saneyoshi T., Kume S., Amasaki Y., and Mikoshiba K. The Wnt{plus 45 degree rule}calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos. Nature 417 (2002) 295-299
    • (2002) Nature , vol.417 , pp. 295-299
    • Saneyoshi, T.1    Kume, S.2    Amasaki, Y.3    Mikoshiba, K.4
  • 104
    • 0030911979 scopus 로고    scopus 로고
    • Intracellular targeting and homotetramer formation of a truncated inositol 1,4,5-trisphosphate receptor-green fluorescent protein chimera in Xenopus laevis oocytes: Evidence for the involvement of the transmembrane spanning domain in endoplasmic reticulum targeting and homotetramer complex formation
    • Sayers L.G., Miyawaki A., Muto A., Takeshita H., Yamamoto A., Michikawa T., Furuichi T., and Mikoshiba K. Intracellular targeting and homotetramer formation of a truncated inositol 1,4,5-trisphosphate receptor-green fluorescent protein chimera in Xenopus laevis oocytes: Evidence for the involvement of the transmembrane spanning domain in endoplasmic reticulum targeting and homotetramer complex formation. Biochem. J. 323 (1997) 273-280
    • (1997) Biochem. J. , vol.323 , pp. 273-280
    • Sayers, L.G.1    Miyawaki, A.2    Muto, A.3    Takeshita, H.4    Yamamoto, A.5    Michikawa, T.6    Furuichi, T.7    Mikoshiba, K.8
  • 105
    • 0033166245 scopus 로고    scopus 로고
    • Protein kinase C is differentially stimulated by Wnt and Frizzled homologs in a G-protein-dependent manner
    • Sheldahl L.C., Park M., Malbon C.C., and Moon R.T. Protein kinase C is differentially stimulated by Wnt and Frizzled homologs in a G-protein-dependent manner. Curr. Biol. 9 (1999) 695-698
    • (1999) Curr. Biol. , vol.9 , pp. 695-698
    • Sheldahl, L.C.1    Park, M.2    Malbon, C.C.3    Moon, R.T.4
  • 106
    • 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. Interaction of Wnt and a Frizzled homologue triggers G-protein-linked phosphatidylinositol signaling. Nature 390 (1997) 410-413
    • (1997) Nature , vol.390 , pp. 410-413
    • Slusarski, D.C.1    Corces, V.G.2    Moon, R.T.3
  • 107
    • 0031080919 scopus 로고    scopus 로고
    • Modulation of embryonic intracellular Ca2+ signaling by Wnt-5A
    • Slusarski D.C., Yang-Snyder J., Busa W.B., and Moon R.T. Modulation of embryonic intracellular Ca2+ signaling by Wnt-5A. Dev. Biol. 182 (1997) 114-120
    • (1997) Dev. Biol. , vol.182 , pp. 114-120
    • Slusarski, D.C.1    Yang-Snyder, J.2    Busa, W.B.3    Moon, R.T.4
  • 108
    • 0029148125 scopus 로고
    • Primaquine, an inhibitor of vesicular transport, blocks the calcium-release-activated current in rat megakaryocytes
    • Somasundaram B., Norman J.C., and Mahaut-Smith M.P. Primaquine, an inhibitor of vesicular transport, blocks the calcium-release-activated current in rat megakaryocytes. Biochem. J. 309 (1995) 725-729
    • (1995) Biochem. J. , vol.309 , pp. 725-729
    • Somasundaram, B.1    Norman, J.C.2    Mahaut-Smith, M.P.3
  • 110
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306 (1983) 67-69
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 111
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler E.E., and Zacharias D.A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81 (2001) 21-50
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 116
    • 0035949497 scopus 로고    scopus 로고
    • Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes
    • Vazquez G., Lievremont J.P., Bird G., and Putney Jr. J.W. Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes. Proc. Natl. Acad. Sci. USA 98 (2001) 11777-11782
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11777-11782
    • Vazquez, G.1    Lievremont, J.P.2    Bird, G.3    Putney Jr., J.W.4
  • 117
    • 0041695485 scopus 로고    scopus 로고
    • A second canon: Functions and mechanisms review of beta-catenin-independent Wnt signaling
    • Veeman M.T., Axelrod J.D., and Moon R.T. A second canon: Functions and mechanisms review of beta-catenin-independent Wnt signaling. Developmental Cell 5 (2003) 1-20
    • (2003) Developmental Cell , vol.5 , pp. 1-20
    • Veeman, M.T.1    Axelrod, J.D.2    Moon, R.T.3
  • 118
    • 0037787872 scopus 로고    scopus 로고
    • Calcium signalling during embryonic development
    • Webb S.E., and Miller A.L. Calcium signalling during embryonic development. Nat. Rev. Mol. Cell. Biol. 4 (2003) 539-551
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 539-551
    • Webb, S.E.1    Miller, A.L.2
  • 119
    • 0033967150 scopus 로고    scopus 로고
    • Calcium signalling during zebrafish embryonic development
    • Webb S.E., and Miller A.L. Calcium signalling during zebrafish embryonic development. Bioessays 22 (2000) 113-123
    • (2000) Bioessays , vol.22 , pp. 113-123
    • Webb, S.E.1    Miller, A.L.2
  • 120
    • 0026582570 scopus 로고
    • Mechanism of inhibition of the calcium pump of sarcoplasmic reticulum by thapsigargin
    • Wictome M., Henderson I., Lee A.G., and East J.M. Mechanism of inhibition of the calcium pump of sarcoplasmic reticulum by thapsigargin. Biochem. J. 283 (1992) 525-529
    • (1992) Biochem. J. , vol.283 , pp. 525-529
    • Wictome, M.1    Henderson, I.2    Lee, A.G.3    East, J.M.4
  • 122
    • 0035043954 scopus 로고    scopus 로고
    • Intracellular signaling mechanisms activated by cholecystokinin-regulating synthesis and secretion of digestive enzymes in pancreatic acinar cells
    • Williams J.A. Intracellular signaling mechanisms activated by cholecystokinin-regulating synthesis and secretion of digestive enzymes in pancreatic acinar cells. Annu. Rev. Physiol. 63 (2001) 77-97
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 77-97
    • Williams, J.A.1
  • 123
    • 0032406715 scopus 로고    scopus 로고
    • Mechanisms of Wnt signaling in development
    • Wodarz A., and Nusse R. Mechanisms of Wnt signaling in development. Annu. Rev. Cell Dev. Biol. 14 (1998) 59-88
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 59-88
    • Wodarz, A.1    Nusse, R.2
  • 125
    • 0037053382 scopus 로고    scopus 로고
    • Calcium influx factor from cytochrome P-450 metabolism and secretion-like coupling mechanisms for capacitative calcium entry in corneal endothelial cells
    • Xie Q., Zhang Y., Zhai C., and Bonanno J.A. Calcium influx factor from cytochrome P-450 metabolism and secretion-like coupling mechanisms for capacitative calcium entry in corneal endothelial cells. J. Biol. Chem. 277 (2002) 16559-16566
    • (2002) J. Biol. Chem. , vol.277 , pp. 16559-16566
    • Xie, Q.1    Zhang, Y.2    Zhai, C.3    Bonanno, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.