메뉴 건너뛰기




Volumn 2, Issue 10, 2007, Pages 652-655

Signaling by committee: Receptor clusters determine pathways of cellular activation

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENOL; ANTIBODY; AUTACOID; BOVINE SERUM ALBUMIN; CALCIUM ION; CELL SURFACE RECEPTOR; DOUBLE STRANDED DNA; FC RECEPTOR; IMMUNOGLOBULIN E; LIGAND; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN KINASE SYK;

EID: 35949004486     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb700214x     Document Type: Article
Times cited : (10)

References (18)
  • 1
    • 0028838012 scopus 로고
    • Dimerization of cell-surface receptors in signal-transduction
    • Heldin, C. H. (1995) Dimerization of cell-surface receptors in signal-transduction, Cell 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 2
    • 33746296180 scopus 로고    scopus 로고
    • Synthetic multivalent ligands as probes of signal tmnsduction
    • Kiessling, L. L., Gestwicki, J. E., and Strong, L. E. (2006) Synthetic multivalent ligands as probes of signal tmnsduction, Angew. Chem., Int. Ed. 45, 2348-2368.
    • (2006) Angew. Chem., Int. Ed , vol.45 , pp. 2348-2368
    • Kiessling, L.L.1    Gestwicki, J.E.2    Strong, L.E.3
  • 3
    • 35948938109 scopus 로고    scopus 로고
    • Trivalent ligands with rigid DNA spacers reveal structural requirements for IgE receptor signaling in RBL mast cells
    • Sil, D. L, Jong, B. L., Luo, D., Holowka, D., and Baird, B. (2007) Trivalent ligands with rigid DNA spacers reveal structural requirements for IgE receptor signaling in RBL mast cells, ACS Chem. Biol. 2, XXX-XXX.
    • (2007) ACS Chem. Biol , vol.2
    • Sil, D.L.1    Jong, B.L.2    Luo, D.3    Holowka, D.4    Baird, B.5
  • 4
    • 34248157158 scopus 로고    scopus 로고
    • Insights into immunoglobulin E receptor signaling from structurally defined ligands
    • Holowka, D., Sil, D., Torigoe, C, and Baird, B. (2007) Insights into immunoglobulin E receptor signaling from structurally defined ligands, Immunol. Rev. 217, 269-279.
    • (2007) Immunol. Rev , vol.217 , pp. 269-279
    • Holowka, D.1    Sil, D.2    Torigoe, C.3    Baird, B.4
  • 5
    • 34247572895 scopus 로고    scopus 로고
    • New developments in Fc epsilon RI regulation, function and inhibition
    • Kraft, S., and Kinet, J. P. (2007) New developments in Fc epsilon RI regulation, function and inhibition, Nat. Rev. Immunol. 7, 365-378.
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 365-378
    • Kraft, S.1    Kinet, J.P.2
  • 6
    • 33344470236 scopus 로고    scopus 로고
    • Integrated signalling pathways for mast-cell activation
    • Gilfillan, A. M., and Tkaczyk, C. (2006) Integrated signalling pathways for mast-cell activation, Nat. Rev. Immunol. 6, 218-230.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 218-230
    • Gilfillan, A.M.1    Tkaczyk, C.2
  • 7
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. (2003) The state of lipid rafts: from model membranes to cells, Annu. Rev. Biophys. Biomol. Struct. 32, 257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 8
    • 0038827018 scopus 로고    scopus 로고
    • A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation
    • Young, R. M., Holowka, D., and Baird, B. (2003) A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation, J. Biol. Chem. 278, 20746-20752.
    • (2003) J. Biol. Chem , vol.278 , pp. 20746-20752
    • Young, R.M.1    Holowka, D.2    Baird, B.3
  • 9
    • 0034744443 scopus 로고    scopus 로고
    • Fc epsilon RI as a paradigm for a lipid raft-dependent receptor in hematopoietic cells
    • Holowka, D., and Baird, B, (2001) Fc epsilon RI as a paradigm for a lipid raft-dependent receptor in hematopoietic cells, Semin. Immunol. 13, 99-105.
    • (2001) Semin. Immunol , vol.13 , pp. 99-105
    • Holowka, D.1    Baird, B.2
  • 10
    • 0018199713 scopus 로고
    • IgE-mast cell system as a paradigm for study of antibody mechanisms
    • Metzger, H. (1978) IgE-mast cell system as a paradigm for study of antibody mechanisms, Immunol. Rev. 41, 186-199.
    • (1978) Immunol. Rev , vol.41 , pp. 186-199
    • Metzger, H.1
  • 11
    • 0022590784 scopus 로고
    • Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
    • Menon, A. K., Holowka, D., Webb, W. W., and Baird, B. (1986) Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization, J. Cell Biol. 102, 541-550.
    • (1986) J. Cell Biol , vol.102 , pp. 541-550
    • Menon, A.K.1    Holowka, D.2    Webb, W.W.3    Baird, B.4
  • 12
    • 0037100419 scopus 로고    scopus 로고
    • Bivalent ligands with rigid double-stranded DNA spacers reveal structural constraints on signaling by Fc epsilon RI
    • Paar, J. M., Harris, N. T., Holowka, D., and Baird, B. (2002) Bivalent ligands with rigid double-stranded DNA spacers reveal structural constraints on signaling by Fc epsilon RI, J. Immunol. 169, 856-864.
    • (2002) J. Immunol , vol.169 , pp. 856-864
    • Paar, J.M.1    Harris, N.T.2    Holowka, D.3    Baird, B.4
  • 13
    • 0346981999 scopus 로고    scopus 로고
    • Influencing receptor-ligand binding mechanisms with multivalent ligand architecture
    • Gestwicki, J. E., Cairo, C. W., Strong, L. E., Oetjen, K. A., and Kiessling, L. L. (2002) Influencing receptor-ligand binding mechanisms with multivalent ligand architecture, J. Am. Chem. Soc. 124, 14922-14933.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 14922-14933
    • Gestwicki, J.E.1    Cairo, C.W.2    Strong, L.E.3    Oetjen, K.A.4    Kiessling, L.L.5
  • 14
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M., and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors, Biochem. J. 351, 95-105.
    • (2000) Biochem. J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 15
    • 0030998836 scopus 로고    scopus 로고
    • Phospholipase C inhibitor, U73122, releases intracellular Ca2+, potentiates Ins(1,4,5)P-3-mediated Ca2+ release and directly activates ion channels in mouse pancreatic acinar cells
    • Mogami, H., Mills, C. L, and Gallagher, D. V. (1997) Phospholipase C inhibitor, U73122, releases intracellular Ca2+, potentiates Ins(1,4,5)P-3-mediated Ca2+ release and directly activates ion channels in mouse pancreatic acinar cells, Biochem. J. 324, 645-651.
    • (1997) Biochem. J , vol.324 , pp. 645-651
    • Mogami, H.1    Mills, C.L.2    Gallagher, D.V.3
  • 16
    • 0033621154 scopus 로고    scopus 로고
    • Heightened sensitivity of a lattice of membrane receptors
    • Duke, T. A., and Bray, D. (1999) Heightened sensitivity of a lattice of membrane receptors, Proc. Natl. Acad. Sci. U.S.A. 96, 10104-10108.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 10104-10108
    • Duke, T.A.1    Bray, D.2
  • 17
    • 35948933303 scopus 로고    scopus 로고
    • Conformational spread in ring of proteins: A generic mechanism of allosteric switching
    • Duke, T., and Bray, D. (2001) Conformational spread in ring of proteins: a generic mechanism of allosteric switching, Biophys. J. 80, 248A-248A.
    • (2001) Biophys. J , vol.80
    • Duke, T.1    Bray, D.2
  • 18
    • 0030834849 scopus 로고    scopus 로고
    • Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking
    • Shea, L D., Omann, G. M., and Linderman, J. J. (1997) Calculation of diffusion-limited kinetics for the reactions in collision coupling and receptor cross-linking, Biophys. J. 73, 2949-2959.
    • (1997) Biophys. J , vol.73 , pp. 2949-2959
    • Shea, L.D.1    Omann, G.M.2    Linderman, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.