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Volumn 706, Issue , 2010, Pages 157-166

Signal transduction mediated through adhesion-GPCRs

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR 56; MEMBRANE PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR; UNCLASSIFIED DRUG;

EID: 79960800882     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-7913-1_14     Document Type: Article
Times cited : (8)

References (52)
  • 1
    • 53149135394 scopus 로고    scopus 로고
    • Adhesion-GPCRs: Emerging roles for novel receptors
    • Yona S, Lin HH, Siu WO et al. Adhesion-GPCRs: Emerging roles for novel receptors. Trends Biochem Sci 2008; 33:491-500.
    • (2008) Trends Biochem Sci , vol.33 , pp. 491-500
    • Yona, S.1    Lin, H.H.2    Siu, W.O.3
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom MC, Schioth HB. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 2008; 7:339-357.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 3
    • 0141923864 scopus 로고    scopus 로고
    • The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans
    • DOI 10.1182/blood-2002-11-3540
    • Stacey M, Chang GW, Davies JQ et al. The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood 2003; 102:2916-2924. (Pubitemid 37248865)
    • (2003) Blood , vol.102 , Issue.8 , pp. 2916-2924
    • Stacey, M.1    Chang, G.-W.2    Davies, J.Q.3    Kwakkenbos, M.J.4    Sanderson, R.D.5    Hamann, J.6    Gordon, S.7    Lin, H.-H.8
  • 4
    • 0035374837 scopus 로고    scopus 로고
    • Human epidermal growth factor (EGF) module-containing mucin-like hormone receptor 3 is a new member of the EGF-TM7 family that recognizes a ligand on human macrophages and activated neutrophils
    • Stacey M, Lin HH, Hilyard KL et al. Human epidermal growth factor (EGF) module-containing mucin-like hormone receptor 3 is a new member of the EGF-TM7 family that recognizes a ligand on human macrophages and activated neutrophils. J Biol Chem 2001; 276:18863-18870.
    • (2001) J Biol Chem , vol.276 , pp. 18863-18870
    • Stacey, M.1    Lin, H.H.2    Hilyard, K.L.3
  • 5
    • 0037047359 scopus 로고    scopus 로고
    • EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20
    • Stacey M, Chang GW, Sanos SL et al. EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20. J Biol Chem 2002; 277:29283-29293.
    • (2002) J Biol Chem , vol.277 , pp. 29283-29293
    • Stacey, M.1    Chang, G.W.2    Sanos, S.L.3
  • 7
    • 0031922202 scopus 로고    scopus 로고
    • Characterization of the CD55 (DAF)-binding site on the seven-span transmembrane receptor CD97
    • DOI 10.1002/(SICI)1521-4141(199805)28:05<1701::AID-IMMU1701>3.0. CO;2-2
    • Hamann J, Stortelers C, Kiss-Toth E et al. Characterization of the CD55 (DAF)-binding site on the seven-span transmembrane receptor CD97. Eur J Immunol 1998; 28:1701-1707. (Pubitemid 28221175)
    • (1998) European Journal of Immunology , vol.28 , Issue.5 , pp. 1701-1707
    • Hamann, J.1    Stortelers, C.2    Kiss-Toth, E.3    Vogel, B.4    Eichler, W.5    Van Lier, R.A.W.6
  • 8
    • 0035968317 scopus 로고    scopus 로고
    • Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: Dissection of the CD97-CD55 complex
    • Lin HH, Stacey M, Saxby C et al. Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: Dissection of the CD97-CD55 complex. J Biol Chem 2001; 276:24160-24169.
    • (2001) J Biol Chem , vol.276 , pp. 24160-24169
    • Lin, H.H.1    Stacey, M.2    Saxby, C.3
  • 16
    • 65249085110 scopus 로고    scopus 로고
    • Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors
    • Silva JP, Lelianova V, Hopkins C et al. Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors. J Biol Chem 2009; 284:6495-506.
    • (2009) J Biol Chem , vol.284 , pp. 6495-506
    • Silva, J.P.1    Lelianova, V.2    Hopkins, C.3
  • 19
    • 0035976990 scopus 로고    scopus 로고
    • A-Latrotoxin, acting via two Ca2*-dependent pathways, triggers exocytosis of two pools of synaptic vesicles
    • Ashton AC, Volynski KE, Lelianova VG et al. a-Latrotoxin, acting via two Ca2*-dependent pathways, triggers exocytosis of two pools of synaptic vesicles. J Biol Chem 2001; 276:44695-44703.
    • (2001) J Biol Chem , vol.276 , pp. 44695-44703
    • Ashton, A.C.1    Volynski, K.E.2    Lelianova, V.G.3
  • 20
    • 0038718789 scopus 로고    scopus 로고
    • N4C enhances spontaneous and evoked transmitter release in CA3 pyramidal neurons
    • Capogna M, Volynski KE, Emptage NJ et al. The a-latrotoxin mutant LTXN4C enhances spontaneous and evoked transmitter release in CA3 pyramidal neurons. J Neurosci 2003; 23:4044-4053. (Pubitemid 36958423)
    • (2003) Journal of Neuroscience , vol.23 , Issue.10 , pp. 4044-4053
    • Capogna, M.1    Volynski, K.E.2    Emptage, N.J.3    Ushkaryov, Y.A.4
  • 23
    • 47249103800 scopus 로고    scopus 로고
    • Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Ga12/13 and Rho pathway
    • Iguchi T, Sakata K, Yoshizaki K et al. Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Ga12/13 and Rho pathway. J Biol Chem 2008; 283:14469-14478.
    • (2008) J Biol Chem , vol.283 , pp. 14469-14478
    • Iguchi, T.1    Sakata, K.2    Yoshizaki, K.3
  • 28
    • 0036033424 scopus 로고    scopus 로고
    • Constitutive activity of G-proteins-coupled receptors: Cause of disease and common property of wild-type receptors
    • DOI 10.1007/s00210-002-0588-0
    • Seifert, R, Wenzel-Seifert K. Constitutive activity of G-protein-coupled receptors: Cause of disease and common property of wild-type receptors. Naunyn Schmiedebergs Arch Pharmacol 2002; 366:381-416. (Pubitemid 35251788)
    • (2002) Naunyn-Schmiedeberg's Archives of Pharmacology , vol.366 , Issue.5 , pp. 381-416
    • Seifert, R.1    Wenzel-Seifert, K.2
  • 29
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum DM, Rasmussen SG, Kobilka BK. The structure and function of G-protein-coupled receptors. Nature 2009; 459:356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 30
    • 33750502435 scopus 로고    scopus 로고
    • Do orphan G-protein-coupled receptors have ligand-independent functions? New insights from receptor heterodimers
    • DOI 10.1038/sj.embor.7400838, PII 7400838
    • Levoye A, Dam J, Ayoub MA et al. Do orphan G-protein-coupled receptors have ligand-independent functions? New insights from receptor heterodimers. EMBO Rep 2006; 7:1094-1098. (Pubitemid 44660563)
    • (2006) EMBO Reports , vol.7 , Issue.11 , pp. 1094-1098
    • Levoye, A.1    Dam, J.2    Ayoub, M.A.3    Guillaume, J.-L.4    Jockers, R.5
  • 31
    • 34848813593 scopus 로고    scopus 로고
    • The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors
    • DOI 10.1074/jbc.M704096200
    • Davies JQ, Chang GW, Yona S et al. The role of receptor oligomerization in modulating the expression and function of leukocyte adhesion-G protein-coupled receptors. J Biol Chem 2007; 282:27343-27353. (Pubitemid 47501907)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 27343-27353
    • Davies, J.Q.1    Chang, G.-W.2    Yona, S.3    Gordon, S.4    Stacey, M.5    Lin, H.-H.6
  • 32
    • 71449087282 scopus 로고    scopus 로고
    • Splicing variants of the orphan G-protein-coupled receptor GPR56 regulate the activity of transcription factors associated with tumorigenesis
    • Kim JE, Han JM, Park CR et al. Splicing variants of the orphan G-protein-coupled receptor GPR56 regulate the activity of transcription factors associated with tumorigenesis. J Cancer Res Clin Oncol 2010; 136:47-53.
    • (2010) J Cancer Res Clin Oncol , vol.136 , pp. 47-53
    • Kim, J.E.1    Han, J.M.2    Park, C.R.3
  • 33
    • 0034636863 scopus 로고    scopus 로고
    • 13α-induced serum response element-dependent transcription
    • DOI 10.1074/jbc.M908449199
    • Shi CS, Sinnarajah S, Cho H et al. G13a-mediated PYK2 activation. PYK2 is a mediator of G13a -induced serum response element-dependent transcription. J Biol Chem 2000; 275:24470-24476. (Pubitemid 30626539)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24470-24476
    • Shi, C.-S.1    Sinnarajah, S.2    Cho, H.3    Kozasa, T.4    Kehrl, J.H.5
  • 34
    • 0028085776 scopus 로고
    • Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gpy-mediated signaling
    • Koch WJ, Hawes BE, Inglese J et al. Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gpy-mediated signaling. J Biol Chem 1994; 269:6193-6197.
    • (1994) J Biol Chem , vol.269 , pp. 6193-6197
    • Koch, W.J.1    Hawes, B.E.2    Inglese, J.3
  • 35
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein
    • Katada T, Ui M. Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc Natl Acad Sci USA 1982; 79:3129-3133.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 36
    • 0020541131 scopus 로고
    • Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via α-adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells
    • Kurose H, Katada T, Amano T et al. Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via a-adrenergic, cholinergic and opiate receptors in neuroblastoma x glioma hybrid cells. J Biol Chem 1983; 258:4870-4875. (Pubitemid 13096378)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.8 , pp. 4870-4875
    • Kurose, H.1    Katada, T.2    Amano, T.3    Ui, M.4
  • 37
    • 9144273884 scopus 로고    scopus 로고
    • Taniguchi metal.anovelgaq/ll-selective inhibitor
    • TakasakiJ,SaitoT,TaniguchiMetal.AnovelGaq/ll-selective inhibitor. JBiolChem2004; 279:47438-47445.
    • (2004) JBiolChem , vol.279 , pp. 47438-47445
    • Takasaki, J.1    Saito, T.2
  • 38
    • 0028225294 scopus 로고
    • 1-adrenoceptor with positive chronotropic effect
    • Magnusson Y, Wallukat G, Waagstein F et al. Autoimmunity in idiopathic dilated cardiomyopathy. Characterization of antibodies against the p 1-adrenoceptor with positive chronotropic effect. Circulation 1994; 89:2760-2767. (Pubitemid 24173697)
    • (1994) Circulation , vol.89 , Issue.6 , pp. 2760-2767
    • Magnusson, Y.1    Wallukat, G.2    Waagstein, F.3    Hjalmarson, A.4    Hoebeke, J.5
  • 43
    • 35948945305 scopus 로고    scopus 로고
    • TSH receptor antibodies
    • DOI 10.1089/thy.2007.0239
    • Smith BR, Sanders J, Furmaniak J. TSH receptor antibodies. Thyroid 2007; 17:923-938. (Pubitemid 350071602)
    • (2007) Thyroid , vol.17 , Issue.10 , pp. 923-938
    • Smith, B.R.1    Sanders, J.2    Furmaniak, J.3
  • 44
    • 34247388037 scopus 로고    scopus 로고
    • Protease-activated receptor signalling, endocytic sorting and dysregulation in cancer
    • DOI 10.1242/jcs.03409
    • Arora P, Ricks TK, Trejo J. Protease-activated receptor signalling, endocytic sorting and dysregulation in cancer. J Cell Sci 2007; 120:921-928. (Pubitemid 46638507)
    • (2007) Journal of Cell Science , vol.120 , Issue.6 , pp. 921-928
    • Arora, P.1    Ricks, T.K.2    Trejo, J.3
  • 47
    • 42149178419 scopus 로고    scopus 로고
    • Differential role of CD97 in interleukin-8-induced and granulocyte-colony stimulating factor-induced hematopoietic stem and progenitor cell mobilization
    • DOI 10.3324/haematol.11606
    • van Pel M, Hagoort H, Kwakkenbos MJ et al. Differential role of CD97 in interleukin-8-induced and granulocyte-colony stimulating factor-induced hematopoietic stem and progenitor cell mobilization. Haematologica 2008; 93:601-604. (Pubitemid 351536390)
    • (2008) Haematologica , vol.93 , Issue.4 , pp. 601-604
    • Van Pel, M.1    Hagoort, H.2    Kwakkenbos, M.J.3    Hamann, J.4    Fibbe, W.E.5
  • 48
    • 58749090038 scopus 로고    scopus 로고
    • Analysis of CD97 expression and manipulation: Antibody treatment but not gene targeting curtails granulocyte migration
    • Veninga H, Becker S, Hoek RM et al. Analysis of CD97 expression and manipulation: Antibody treatment but not gene targeting curtails granulocyte migration. J Immunol 2008; 181:6574-6583.
    • (2008) J Immunol , vol.181 , pp. 6574-6583
    • Veninga, H.1    Becker, S.2    Hoek, R.M.3
  • 50
    • 36048988253 scopus 로고    scopus 로고
    • Individual cell-based models of tumor-environment interactions: Multiple effects of CD97 on tumor invasion
    • DOI 10.2353/ajpath.2006.060006
    • Galle J, Sittig D, Hanisch I et al. Individual cell-based models of tumor-environment interactions: Multiple effects of CD97 on tumor invasion. Am J Pathol 2006; 169:1802-1811. (Pubitemid 351182009)
    • (2006) American Journal of Pathology , vol.169 , Issue.5 , pp. 1802-1811
    • Galle, J.1    Sittig, D.2    Hanisch, I.3    Wobus, M.4    Wandel, E.5    Loeffler, M.6    Aust, G.7
  • 52
    • 2542603008 scopus 로고    scopus 로고
    • Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein
    • DOI 10.1038/sj.onc.1207495
    • Yamamoto Y, Irie K, Asada M et al. Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5) and a novel TEM5-like protein. Oncogene 2004; 23:3889-3897. (Pubitemid 38747917)
    • (2004) Oncogene , vol.23 , Issue.22 , pp. 3889-3897
    • Yamamoto, Y.1    Irie, K.2    Asada, M.3    Mino, A.4    Mandai, K.5    Takai, Y.6


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