메뉴 건너뛰기




Volumn 6, Issue 6, 2014, Pages 727-738

Termination of immune activation: An essential component of healthy host immune responses

Author keywords

Endocytosis; Immunoreceptor tyrosine based activation motifs; Immunoreceptor tyrosine based inhibitory motifs; Intracellular signalling; Leucocyte immunoglobulin like receptors; Ubiquitination

Indexed keywords

ADAPTOR PROTEIN;

EID: 84908653786     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000363449     Document Type: Review
Times cited : (17)

References (99)
  • 1
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M: Antigen receptor tail clue. Nature 1989; 338:383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 2
    • 28544438330 scopus 로고    scopus 로고
    • Role of ITAM-containing adapter proteins and their receptors in the immune system and bone
    • Humphrey MB, Lanier LL, Nakamura MC: Role of ITAM-containing adapter proteins and their receptors in the immune system and bone. Immunol Rev 2005; 208:50-65.
    • (2005) Immunol Rev , vol.208 , pp. 50-65
    • Humphrey, M.B.1    Lanier, L.L.2    Nakamura, M.C.3
  • 3
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyro-sine kinases in immunoreceptor signaling
    • Latour S, Veillette A: Proximal protein tyro-sine kinases in immunoreceptor signaling. Curr Opin Immunol 2001; 13:299-306.
    • (2001) Curr Opin Immunol , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 4
    • 84879215735 scopus 로고    scopus 로고
    • Phosphatase regulation of immunorecep-tor signaling in T cells, B cells and mast cells
    • Bounab Y, Getahun A, Cambier J.C., Daëron M: Phosphatase regulation of immunorecep-tor signaling in T cells, B cells and mast cells. Curr Opin Immunol 2013; 25:313-320.
    • (2013) Curr Opin Immunol , vol.25 , pp. 313-320
    • Bounab, Y.1    Getahun, A.2    Cambier, J.C.3    Daëron, M.4
  • 5
    • 30944435657 scopus 로고    scopus 로고
    • Signaling by ITIM-bearing receptors
    • Verbrugge A, Meyaard L: Signaling by ITIM-bearing receptors. Curr Immunol Rev 2005; 1: 201-212.
    • (2005) Curr Immunol Rev , vol.1 , pp. 201-212
    • Verbrugge, A.1    Meyaard, L.2
  • 6
    • 33644688070 scopus 로고    scopus 로고
    • ITAM-based signalling beyond the adaptive immune response
    • Foddor S, Jakus Z, Mocsai A: ITAM-based signalling beyond the adaptive immune response. Immunol Lett 2006; 104:29-37.
    • (2006) Immunol Lett , vol.104 , pp. 29-37
    • Foddor, S.1    Jakus, Z.2    Mocsai, A.3
  • 7
    • 0346725003 scopus 로고    scopus 로고
    • Systematic identification of immunoreceptor tyro-sine-based inhibitory motifs in the human proteome
    • Staub E, Rosenthal A, Hinzmann B: Systematic identification of immunoreceptor tyro-sine-based inhibitory motifs in the human proteome. Cell Signal 2004; 16:435-456.
    • (2004) Cell Signal , vol.16 , pp. 435-456
    • Staub, E.1    Rosenthal, A.2    Hinzmann, B.3
  • 8
    • 4344677515 scopus 로고    scopus 로고
    • The LILR family: Modulators of innate and adaptive immune pathways in health and disease
    • Brown D, Trowsdale J, Allen R: The LILR family: modulators of innate and adaptive immune pathways in health and disease. Tissue Antigens 2004; 64:215-225.
    • (2004) Tissue Antigens , vol.64 , pp. 215-225
    • Brown, D.1    Trowsdale, J.2    Allen, R.3
  • 9
    • 0034118795 scopus 로고    scopus 로고
    • LIRs/ILTs/MIRs, inhibitory and stimulatory igsuperfamily receptors expressed in myeloid and lymphoid cells
    • Borges L, Cosman D: LIRs/ILTs/MIRs, inhibitory and stimulatory Igsuperfamily receptors expressed in myeloid and lymphoid cells. Cyto-kine Growth Factor Rev 2000; 11: 209-217.
    • (2000) Cyto-kine Growth Factor Rev , vol.11 , pp. 209-217
    • Borges, L.1    Cosman, D.2
  • 10
    • 0032813723 scopus 로고    scopus 로고
    • The leukocyte immunoglobulin-like receptors (LIRs): A new family of immune regulators
    • Fanger N, Borges L, Cosman D: The leukocyte immunoglobulin-like receptors (LIRs): a new family of immune regulators. J Leukoc Biol 1999; 66:231-236.
    • (1999) J Leukoc Biol , vol.66 , pp. 231-236
    • Fanger, N.1    Borges, L.2    Cosman, D.3
  • 11
    • 0032607844 scopus 로고    scopus 로고
    • Cutting edge: Human myeloid cells express an activating ILT receptor (ILT1) that associates with fc receptor γ-chain
    • Nakajima H, Samaridis J, Angman L., Colon-na M: Cutting edge: human myeloid cells express an activating ILT receptor (ILT1) that associates with Fc receptor γ-chain. J Immunol 1999; 162:5-8.
    • (1999) J Immunol , vol.162 , pp. 5-8
    • Nakajima, H.1    Samaridis, J.2    Angman, L.3    Colon-Na, M.4
  • 13
    • 0030768392 scopus 로고    scopus 로고
    • A novel immuno-globulin superfamily receptor for cellular and viral MHC class I molecules
    • Cosman D, Fanger N, Borges L., Kubin M, Chin W, Peterson L., et al.: A novel immuno-globulin superfamily receptor for cellular and viral MHC class I molecules. Immunity 1997; 7:273-282.
    • (1997) Immunity , vol.7 , pp. 273-282
    • Cosman, D.1    Fanger, N.2    Borges, L.3    Kubin, M.4    Chin, W.5    Peterson, L.6
  • 14
    • 77955480482 scopus 로고    scopus 로고
    • Soluble LILRA3, a potential natural antiinflammatory protein, is increased in patients with rheumatoid arthritis and is tightly regulated by Interleukin 10, tumor necrosis factor-alpha, and interferon-gamma
    • An H, Chandra V, Piraino B., Borges L, Geczy C, McNeil H., et al.: Soluble LILRA3, a potential natural antiinflammatory protein, is increased in patients with rheumatoid arthritis and is tightly regulated by interleukin 10, tumor necrosis factor-alpha, and interferon-gamma. J Rheumatol 2010; 37:1596-1606.
    • (2010) J Rheumatol , vol.37 , pp. 1596-1606
    • An, H.1    Chandra, V.2    Piraino, B.3    Borges, L.4    Geczy, C.5    McNeil, H.6
  • 15
    • 26444459466 scopus 로고    scopus 로고
    • Extensive polymorphisms of LILRB1 (ILT2, LIR1) and their association with HLA-DRB1 shared epi-tope negative rheumatoid arthritis
    • Kuroki K, Tsuchiya N, Shiroishi M., Rasubala L, Yamashita Y, Matsuta K., et al.: Extensive polymorphisms of LILRB1 (ILT2, LIR1) and their association with HLA-DRB1 shared epi-tope negative rheumatoid arthritis. Hum Mol Genet 2005; 14:2469-2480.
    • (2005) Hum Mol Genet , vol.14 , pp. 2469-2480
    • Kuroki, K.1    Tsuchiya, N.2    Shiroishi, M.3    Rasubala, L.4    Yamashita, Y.5    Matsuta, K.6
  • 16
    • 34548522452 scopus 로고    scopus 로고
    • Analysis of expression and function of the inhibitory receptor ILT2 (CD85j/LILRB1/LIR-1) in peripheral blood mononuclear cells from patients with systemic lupus erythematosus (SLE)
    • Monsivais-Urenda A, Nino-Moreno P, Abud-Mendoza C, Baranda L, Layseca-Espi-nosa E, Lopez-Botet M, et al.: Analysis of expression and function of the inhibitory receptor ILT2 (CD85j/LILRB1/LIR-1) in peripheral blood mononuclear cells from patients with systemic lupus erythematosus (SLE). J Autoimmun 2007; 29:97-105.
    • (2007) J Autoimmun , vol.29 , pp. 97-105
    • Monsivais-Urenda, A.1    Nino-Moreno, P.2    Abud-Mendoza, C.3    Baranda, L.4    Layseca-Espi-Nosa, E.5    Lopez-Botet, M.6
  • 18
    • 79952419540 scopus 로고    scopus 로고
    • Expression of activating and inhibitory Leukocyte immunoglobu-lin-like receptors in rheumatoid synovium: Correlations to disease activity
    • Tedla N, An H, Borges L., Vollmer-Conna U, Bryant K, Geczy C., et al.: Expression of activating and inhibitory leukocyte immunoglobu-lin-like receptors in rheumatoid synovium: correlations to disease activity. Tissue Antigens 2011; 77:305-316.
    • (2011) Tissue Antigens , vol.77 , pp. 305-316
    • Tedla, N.1    An, H.2    Borges, L.3    Vollmer-Conna, U.4    Bryant, K.5    Geczy, C.6
  • 19
    • 78649829502 scopus 로고    scopus 로고
    • Paired NK cell receptors controlling NK cytotoxicity
    • Stanietsky N, Mandelboim O: Paired NK cell receptors controlling NK cytotoxicity. FEBS Lett 2010; 584:4895-4900.
    • (2010) FEBS Lett , vol.584 , pp. 4895-4900
    • Stanietsky, N.1    Mandelboim, O.2
  • 20
    • 37549036732 scopus 로고    scopus 로고
    • Fc γ receptors as regulators of immune responses
    • Nimmerjahn F, Ravetch JV: Fc γ receptors as regulators of immune responses. Nat Rev Immunol 2008; 8:34-47.
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 21
  • 22
    • 84864144129 scopus 로고    scopus 로고
    • CD22 and siglec-G in B cell function and tolerance
    • Poe JC, Tedder TF: CD22 and Siglec-G in B cell function and tolerance. Trends Immunol 2012; 33:413-420.
    • (2012) Trends Immunol , vol.33 , pp. 413-420
    • Poe, J.C.1    Tedder, T.F.2
  • 23
    • 38849203194 scopus 로고    scopus 로고
    • CD22: An inhibitory enigma
    • Walker JA, Smith KGC: CD22: an inhibitory enigma. Immunology 2008; 123:314-325.
    • (2008) Immunology , vol.123 , pp. 314-325
    • Walker, J.A.1    Smith, K.G.C.2
  • 24
    • 84859149168 scopus 로고    scopus 로고
    • LILRA2 selectively modulates LPS-mediated cytokine production and inhibits phagocytosis by monocytes
    • Lu HK, Mitchell A, Endoh Y., Hampartzou-mian T, Huynh O, Borges L., et al.: LILRA2 selectively modulates LPS-mediated cytokine production and inhibits phagocytosis by monocytes. PLoS One 2012; 7:e33478.
    • (2012) PLoS One , vol.7
    • Lu, H.K.1    Mitchell, A.2    Endoh, Y.3    Hampartzou-Mian, T.4    Huynh, O.5    Borges, L.6
  • 25
    • 40049098041 scopus 로고    scopus 로고
    • LILRA2 activation inhibits dendritic cell differentiation and antigen presentation to T cells
    • Lee DJ, Sieling PA, Ochoa M.T., Krutzik SR, Guo B, Hernandez M, et al.: LILRA2 activation inhibits dendritic cell differentiation and antigen presentation to T cells. J Immunol 2007; 179:8128-8136.
    • (2007) J Immunol , vol.179 , pp. 8128-8136
    • Lee, D.J.1    Sieling, P.A.2    Ochoa, M.T.3    Krutzik, S.R.4    Guo, B.5    Hernandez, M.6
  • 26
    • 0141818360 scopus 로고    scopus 로고
    • Use of genetic profiling in leprosy to discriminate clinical forms of the disease
    • Bleharski JR, Li H, Meinken C., Graeber TG, Ochoa MT, Yamamura M, et al.: Use of genetic profiling in leprosy to discriminate clinical forms of the disease. Science 2003; 301: 1527-1530.
    • (2003) Science , vol.301 , pp. 1527-1530
    • Bleharski, J.R.1    Li, H.2    Meinken, C.3    Graeber, T.G.4    Ochoa, M.T.5    Yamamura, M.6
  • 28
    • 19944430878 scopus 로고    scopus 로고
    • Identification of FCαRI as an inhibitory receptor that controls inflammation: Dual role of FcRγ ITAM
    • Pasquier B, Launay P, Kanamaru Y., Moura IC, Pfirsch S, Ruffié C, et al.: Identification of FCαRI as an inhibitory receptor that controls inflammation: dual role of FcRγ ITAM. Immunity 2005; 22:31-42.
    • (2005) Immunity , vol.22 , pp. 31-42
    • Pasquier, B.1    Launay, P.2    Kanamaru, Y.3    Moura, I.C.4    Pfirsch, S.5    Ruffié, C.6
  • 29
    • 81955161811 scopus 로고    scopus 로고
    • Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell an-ergy
    • O'Neill SK, Getahun A, Gauld S.B., Merrell KT, Tamir I, Smith MJ, et al.: Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell an-ergy. Immunity 2011; 35:746-756.
    • (2011) Immunity , vol.35 , pp. 746-756
    • O'Neill, S.K.1    Getahun, A.2    Gauld, S.B.3    Merrell, K.T.4    Tamir, I.5    Smith, M.J.6
  • 30
    • 0033404953 scopus 로고    scopus 로고
    • Partially phosphorylated T cell receptor ζ molecules can inhibit T cell activation
    • Kersh EN, Kersh GJ, Allen PM: Partially phosphorylated T cell receptor ζ molecules can inhibit T cell activation. J Exp Med 1999; 190:1627-1636.
    • (1999) J Exp Med , vol.190 , pp. 1627-1636
    • Kersh, E.N.1    Kersh, G.J.2    Allen, P.M.3
  • 31
    • 84859364858 scopus 로고    scopus 로고
    • IgG1 and IVIg induce inhibitory ITAM signaling through FCγRIII controlling inflammatory responses
    • Aloulou M, Ben Mkaddem S, Biarnes-Pelicot M, Boussetta T., Souchet H, Rossato E, et al.: IgG1 and IVIg induce inhibitory ITAM signaling through FCγRIII controlling inflammatory responses. Blood 2012; 119:3084-3096.
    • (2012) Blood , vol.119 , pp. 3084-3096
    • Aloulou, M.1    Ben Mkaddem, S.2    Biarnes-Pelicot, M.3    Boussetta, T.4    Souchet, H.5    Rossato, E.6
  • 32
    • 33746256913 scopus 로고    scopus 로고
    • You say ITAM and I say ITIM, let's call the whole thing off: The ambiguity of immunoreceptor signalling
    • Barrow AD, Trowsdale J: You say ITAM and I say ITIM, let's call the whole thing off: the ambiguity of immunoreceptor signalling. Eur J Immunol 2006; 36:1646-1653.
    • (2006) Eur J Immunol , vol.36 , pp. 1646-1653
    • Barrow, A.D.1    Trowsdale, J.2
  • 33
    • 20644443886 scopus 로고    scopus 로고
    • Enhanced toll-like receptor responses in the absence of signaling adaptor DAP12
    • Hamerman JA, Tchao NK, Lowell C.A., Lanier LL: Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12. Nat Immunol 2005; 6:579-586.
    • (2005) Nat Immunol , vol.6 , pp. 579-586
    • Hamerman, J.A.1    Tchao, N.K.2    Lowell, C.A.3    Lanier, L.L.4
  • 34
    • 24744455913 scopus 로고    scopus 로고
    • Par-adoxic inhibition of human natural interfer-on-producing cells by the activating receptor NKp44
    • Fuchs A, Cella M, Kondo T., Colonna M: Par-adoxic inhibition of human natural interfer-on-producing cells by the activating receptor NKp44. Blood 2005; 106:2076-2082.
    • (2005) Blood , vol.106 , pp. 2076-2082
    • Fuchs, A.1    Cella, M.2    Kondo, T.3    Colonna, M.4
  • 35
    • 33644772437 scopus 로고    scopus 로고
    • Siglec-H is an IPC-specific receptor that modulates type I IFN secretion through DAP12
    • Blasius AL, Cella M, Maldonado J., Takai T, Colonna M: Siglec-H is an IPC-specific receptor that modulates type I IFN secretion through DAP12. Blood 2006; 107:2474-2476.
    • (2006) Blood , vol.107 , pp. 2474-2476
    • Blasius, A.L.1    Cella, M.2    Maldonado, J.3    Takai, T.4    Colonna, M.5
  • 36
    • 0035496101 scopus 로고    scopus 로고
    • Epstein-barr virus: Exploiting the immune system
    • Thorley-Lawson DA: Epstein-Barr virus: exploiting the immune system. Nat Rev Immunol 2001; 1:75-82.
    • (2001) Nat Rev Immunol , vol.1 , pp. 75-82
    • Thorley-Lawson, D.A.1
  • 37
    • 2442450439 scopus 로고    scopus 로고
    • Cutting edge: Trem-like transcript-1, a platelet immuno-receptor tyrosine-based inhibition motif encoding costimulatory immunoreceptor that enhances, rather than inhibits, calcium signaling via SHP-2
    • Barrow AD, Astoul E, Floto A., Brooke G, Relou IAM, Jennings NS, et al.: Cutting edge: TREM-like transcript-1, a platelet immuno-receptor tyrosine-based inhibition motif encoding costimulatory immunoreceptor that enhances, rather than inhibits, calcium signaling via SHP-2. J Immunol 2004; 172:5838-5842.
    • (2004) J Immunol , vol.172 , pp. 5838-5842
    • Barrow, A.D.1    Astoul, E.2    Floto, A.3    Brooke, G.4    Relou, I.A.M.5    Jennings, N.S.6
  • 38
    • 0037331539 scopus 로고    scopus 로고
    • The human TREM gene cluster at 6p21.1 encodes both activating and inhibitory single IgV domain receptors and includes NKp44
    • Allcock RJN, Barrow AD, Forbes S, Beck S., Trowsdale J: The human TREM gene cluster at 6p21.1 encodes both activating and inhibitory single IgV domain receptors and includes NKp44. Eur J Immunol 2003; 33:567-577.
    • (2003) Eur J Immunol , vol.33 , pp. 567-577
    • Allcock, R.J.N.1    Barrow, A.D.2    Forbes, S.3    Beck, S.4    Trowsdale, J.5
  • 40
    • 20144377821 scopus 로고    scopus 로고
    • A novel mechanism for JAK2 activation by a G protein-coupled receptor, the CCK2R: Implication of this signaling pathway in pancreatic tumor models
    • Ferrand A, Kowalski-Chauvel A, Bertrand C., Escrieut C, Mathieu A, Portolan G., et al.: A novel mechanism for JAK2 activation by a G protein-coupled receptor, the CCK2R: implication of this signaling pathway in pancreatic tumor models. J Biol Chem 2005; 280:10710-10715.
    • (2005) J Biol Chem , vol.280 , pp. 10710-10715
    • Ferrand, A.1    Kowalski-Chauvel, A.2    Bertrand, C.3    Escrieut, C.4    Mathieu, A.5    Portolan, G.6
  • 41
    • 0033575251 scopus 로고    scopus 로고
    • Src-family tyrosine kinases in activation of ERK-1 and p85/p110-phos-phatidylinositol 3-kinase by G/CCKB receptors
    • Daulhac L, Kowalski-Chauvel A, Pradayrol L., Vaysse N, Seva C: Src-family tyrosine kinases in activation of ERK-1 and p85/p110-phos-phatidylinositol 3-kinase by G/CCKB receptors. J Biol Chem 1999; 274:20657-20663.
    • (1999) J Biol Chem , vol.274 , pp. 20657-20663
    • Daulhac, L.1    Kowalski-Chauvel, A.2    Pradayrol, L.3    Vaysse, N.4    Seva, C.5
  • 42
    • 0029860143 scopus 로고    scopus 로고
    • Gastrin stimulates tyrosine phosphor-ylation of insulin receptor substrate 1 and its association with grb2 and the phosphati-dylinositol 3-kinase
    • Kowalski-Chauvel A, Pradayrol L, Vaysse N., Seva C: Gastrin stimulates tyrosine phosphor-ylation of insulin receptor substrate 1 and its association with Grb2 and the phosphati-dylinositol 3-kinase. J Biol Chem 1996; 271: 26356-26361.
    • (1996) J Biol Chem , vol.271 , pp. 26356-26361
    • Kowalski-Chauvel, A.1    Pradayrol, L.2    Vaysse, N.3    Seva, C.4
  • 43
    • 47049125345 scopus 로고    scopus 로고
    • A dual activation and inhibition role for the paired immunoglobulin-like receptor B in eosinophils
    • Munitz A, McBride ML, Bernstein J.S., Rothen-berg ME: A dual activation and inhibition role for the paired immunoglobulin-like receptor B in eosinophils. Blood 2008; 111:5694-5703.
    • (2008) Blood , vol.111 , pp. 5694-5703
    • Munitz, A.1    McBride, M.L.2    Bernstein, J.S.3    Rothen-Berg, M.E.4
  • 44
    • 0035340798 scopus 로고    scopus 로고
    • CD150 association with either the SH2-con-taining inositol phosphatase or the SH2-con-taining protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A
    • Shlapatska LM, Mikhalap SV, Berdova A.G., Zelensky OM, Yun TJ, Nichols KE, et al.: CD150 association with either the SH2-con-taining inositol phosphatase or the SH2-con-taining protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A. J Immunol 2001; 166:5480-5487.
    • (2001) J Immunol , vol.166 , pp. 5480-5487
    • Shlapatska, L.M.1    Mikhalap, S.V.2    Berdova, A.G.3    Zelensky, O.M.4    Yun, T.J.5    Nichols, K.E.6
  • 45
    • 2942530671 scopus 로고    scopus 로고
    • KIR2DL5 can inhibit human NK cell activation via recruitment of src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2)
    • Yusa S, Catina TL, Campbell KS: KIR2DL5 can inhibit human NK cell activation via recruitment of Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2). J Immunol 2004; 172:7385-7392.
    • (2004) J Immunol , vol.172 , pp. 7385-7392
    • Yusa, S.1    Catina, T.L.2    Campbell, K.S.3
  • 46
    • 9144241714 scopus 로고    scopus 로고
    • The membrane-proximal immunorecep-tor tyrosine-based inhibitory motif is critical for the inhibitory signaling mediated by siglecs-7 and -9, CD33-related siglecs expressed on human monocytes and NK cells
    • Avril T, Floyd H, Lopez F., Vivier E, Crocker PR: The membrane-proximal immunorecep-tor tyrosine-based inhibitory motif is critical for the inhibitory signaling mediated by Siglecs-7 and -9, CD33-related Siglecs expressed on human monocytes and NK cells. J Immunol 2004; 173:6841-6849.
    • (2004) J Immunol , vol.173 , pp. 6841-6849
    • Avril, T.1    Floyd, H.2    Lopez, F.3    Vivier, E.4    Crocker, P.R.5
  • 47
    • 3142688997 scopus 로고    scopus 로고
    • SHP-1 and SHP-2 associate with immunoreceptor tyrosine-based switch motif of programmed death 1 upon primary human T cell stimulation, but only receptor ligation prevents T cell activation
    • Chemnitz JM, Parry RV, Nichols K.E., June CH, Riley JL: SHP-1 and SHP-2 associate with immunoreceptor tyrosine-based switch motif of programmed death 1 upon primary human T cell stimulation, but only receptor ligation prevents T cell activation. J Immunol 2004; 173:945-954.
    • (2004) J Immunol , vol.173 , pp. 945-954
    • Chemnitz, J.M.1    Parry, R.V.2    Nichols, K.E.3    June, C.H.4    Riley, J.L.5
  • 48
    • 72749110288 scopus 로고    scopus 로고
    • Discovery of a functional immunoreceptor tyrosine-based switch motif in a 7-transmembrane-spanning receptor: Role in the orexin receptor OX1R-driven apoptosis
    • El Firar A, Voisin T, Rouyer-Fessard C, Ostuni M.A., Couvineau A., Laburthe M: Discovery of a functional immunoreceptor tyrosine-based switch motif in a 7-transmembrane-spanning receptor: role in the orexin receptor OX1R-driven apoptosis. FASEB J 2009; 23: 4069-4080.
    • (2009) FASEB J , vol.23 , pp. 4069-4080
    • El Firar, A.1    Voisin, T.2    Rouyer-Fessard, C.3    Ostuni, M.A.4    Couvineau, A.5    Laburthe, M.6
  • 49
    • 33748848714 scopus 로고    scopus 로고
    • Interleukin-6 biology is coordinated by membrane-bound and soluble receptors: Role in inflammation and cancer
    • Rose-John S, Scheller J, Elson G., Jones SA: Interleukin-6 biology is coordinated by membrane-bound and soluble receptors: role in inflammation and cancer. J Leukoc Biol 2006; 80:227-236.
    • (2006) J Leukoc Biol , vol.80 , pp. 227-236
    • Rose-John, S.1    Scheller, J.2    Elson, G.3    Jones, S.A.4
  • 50
    • 6344268944 scopus 로고    scopus 로고
    • Mechanisms of soluble cytokine receptor generation
    • Levine SJ: Mechanisms of soluble cytokine receptor generation. J Immunol 2004; 173: 5343-5348.
    • (2004) J Immunol , vol.173 , pp. 5343-5348
    • Levine, S.J.1
  • 51
    • 0031879125 scopus 로고    scopus 로고
    • Soluble receptors in human disease
    • Heaney ML, Golde DW: Soluble receptors in human disease. J Leukoc Biol 1998; 64:135-146.
    • (1998) J Leukoc Biol , vol.64 , pp. 135-146
    • Heaney, M.L.1    Golde, D.W.2
  • 52
    • 75549091673 scopus 로고    scopus 로고
    • The IL-1 family: Regulators of immunity
    • Sims JE, Smith DE: The IL-1 family: regulators of immunity. Nat Rev Immunol 2010; 10: 89-102.
    • (2010) Nat Rev Immunol , vol.10 , pp. 89-102
    • Sims, J.E.1    Smith, D.E.2
  • 53
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio M, Ni J, Feng P., Dixit VM: IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 1997; 278:1612-1615.
    • (1997) Science , vol.278 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 54
    • 0029009910 scopus 로고
    • Molecular cloning and characterization of a second subunit of the in-Terleukin 1 receptor complex
    • Greenfeder SA, Nunes P, Kwee L., Labow M, Chizzonite RA, Ju G: Molecular cloning and characterization of a second subunit of the in-terleukin 1 receptor complex. J Biol Chem 1995; 270:13757-13765.
    • (1995) J Biol Chem , vol.270 , pp. 13757-13765
    • Greenfeder, S.A.1    Nunes, P.2    Kwee, L.3    Labow, M.4    Chizzonite, R.A.5    Ju, G.6
  • 55
    • 0027181936 scopus 로고
    • Interleukin-1 type II receptor: A decoy target for IL-1 that is regulated by IL-4
    • Colotta F, Re F, Muzio M., Bertini R, Polenta-rutti N, Sironi M, et al.: Interleukin-1 type II receptor: a decoy target for IL-1 that is regulated by IL-4. Science 1993; 261:472-475.
    • (1993) Science , vol.261 , pp. 472-475
    • Colotta, F.1    Re, F.2    Muzio, M.3    Bertini, R.4    Polenta-Rutti, N.5    Sironi, M.6
  • 56
    • 21644477461 scopus 로고    scopus 로고
    • SIGIRR inhibits Interleukin-1 receptor- and toll-like receptor 4-mediated signaling through different mechanisms
    • Qin J, Qian Y, Yao J., Grace C, Li X: SIGIRR inhibits interleukin-1 receptor- and toll-like receptor 4-mediated signaling through different mechanisms. J Biol Chem 2005; 280: 25233-25241.
    • (2005) J Biol Chem , vol.280 , pp. 25233-25241
    • Qin, J.1    Qian, Y.2    Yao, J.3    Grace, C.4    Li, X.5
  • 57
    • 84871712791 scopus 로고    scopus 로고
    • D6: The 'crowd controller' at the immune gateway
    • Lee KM, Nibbs RJB, Graham GJ: D6: the 'crowd controller' at the immune gateway. Trends Immunol 2013; 34:7-12.
    • (2013) Trends Immunol , vol.34 , pp. 7-12
    • Lee, K.M.1    Nibbs, R.J.B.2    Graham, G.J.3
  • 58
    • 17444424930 scopus 로고    scopus 로고
    • Genomic amplification of a decoy receptor for fas ligand in lung and colon cancer
    • Pitti RM, Marsters SA, Lawrence D.A., Roy M., Kischkel FC, Dowd P, et al.: Genomic amplification of a decoy receptor for Fas ligand in lung and colon cancer. Nature 1998; 396:699-703.
    • (1998) Nature , vol.396 , pp. 699-703
    • Pitti, R.M.1    Marsters, S.A.2    Lawrence, D.A.3    Roy, M.4    Kischkel, F.C.5    Dowd, P.6
  • 59
    • 34548454049 scopus 로고    scopus 로고
    • Biology of RANK, RANKL, and osteoprotegerin
    • Boyce BF, Xing L: Biology of RANK, RANKL, and osteoprotegerin. Arthritis Res Ther 2007; 9(SUPPL. 1):S1.
    • (2007) Arthritis Res Ther , vol.9 , pp. S1
    • Boyce, B.F.1    Xing, L.2
  • 60
    • 0037699954 scopus 로고    scopus 로고
    • The biology of VEGF and its receptors
    • Ferrara N, Gerber H-P, LeCouter J: The biology of VEGF and its receptors. Nat Med 2003; 9:669-676.
    • (2003) Nat Med , vol.9 , pp. 669-676
    • Ferrara, N.1    Gerber, H.-P.2    LeCouter, J.3
  • 61
    • 78650090605 scopus 로고    scopus 로고
    • Ubiquitin makes its mark on immune regulation
    • Malynn BA, Ma A: Ubiquitin makes its mark on immune regulation. Immunity 2010; 33: 843-852.
    • (2010) Immunity , vol.33 , pp. 843-852
    • Malynn, B.A.1    Ma, A.2
  • 62
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun SC: Deubiquitylation and regulation of the immune response. Nat Rev Immunol 2008; 8:501-511.
    • (2008) Nat Rev Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 64
    • 63649116570 scopus 로고    scopus 로고
    • Ubiquitylation in innate and adaptive immunity
    • Bhoj VG, Chen ZJ: Ubiquitylation in innate and adaptive immunity. Nature 2009; 458: 430-437.
    • (2009) Nature , vol.458 , pp. 430-437
    • Bhoj, V.G.1    Chen, Z.J.2
  • 65
    • 62849118323 scopus 로고    scopus 로고
    • Autoregulatory feedback loops terminating the NF-κB response
    • Renner F, Schmitz ML: Autoregulatory feedback loops terminating the NF-κB response. Trends Biochem Sci 2009; 34:128-135.
    • (2009) Trends Biochem Sci , vol.34 , pp. 128-135
    • Renner, F.1    Schmitz, M.L.2
  • 66
    • 43249120917 scopus 로고    scopus 로고
    • Lys63-linked polyubiquitination of IRAK-1 is required for Interleukin-1 receptor- and toll-like receptor-mediated NF-kap-paB activation
    • Conze DB, Wu CJ, Thomas J.A., Landstrom A., Ashwell JD: Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kap-paB activation. Mol Cell Biol 2008; 28:3538-3547.
    • (2008) Mol Cell Biol , vol.28 , pp. 3538-3547
    • Conze, D.B.1    Wu, C.J.2    Thomas, J.A.3    Landstrom, A.4    Ashwell, J.D.5
  • 67
    • 84865404917 scopus 로고    scopus 로고
    • The innate immune sensor NLRC3 attenuates tolllike receptor signaling via modification of the signaling adaptor TRAF6 and transcription factor NF-kappaB
    • Schneider M, Zimmermann AG, Roberts R.A., Zhang L., Swanson KV, Wen H, et al.: The innate immune sensor NLRC3 attenuates Tolllike receptor signaling via modification of the signaling adaptor TRAF6 and transcription factor NF-kappaB. Nat Immunol 2012; 13: 823-831.
    • (2012) Nat Immunol , vol.13 , pp. 823-831
    • Schneider, M.1    Zimmermann, A.G.2    Roberts, R.A.3    Zhang, L.4    Swanson, K.V.5    Wen, H.6
  • 68
    • 79959350721 scopus 로고    scopus 로고
    • NLRX1 protein attenuates inflammatory responses to infection by interfering with the RIG-I-MAVS and TRAF6-NF-kappaB signaling pathways
    • Allen IC, Moore CB, Schneider M, Lei Y., Davis BK, Scull MA, et al.: NLRX1 protein attenuates inflammatory responses to infection by interfering with the RIG-I-MAVS and TRAF6-NF-kappaB signaling pathways. Immunity 2011; 34:854-865.
    • (2011) Immunity , vol.34 , pp. 854-865
    • Allen, I.C.1    Moore, C.B.2    Schneider, M.3    Lei, Y.4    Davis, B.K.5    Scull, M.A.6
  • 69
    • 84861330800 scopus 로고    scopus 로고
    • MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors
    • Castanier C, Zemirli N, Portier A., Garcin D, Bidere N, Vazquez A., et al.: MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors. BMC Biol 2012; 10: 44.
    • (2012) BMC Biol , vol.10 , pp. 44
    • Castanier, C.1    Zemirli, N.2    Portier, A.3    Garcin, D.4    Bidere, N.5    Vazquez, A.6
  • 71
    • 84878232476 scopus 로고    scopus 로고
    • The history of toll-like receptors - Redefining innate immunity
    • O'Neill LA, Golenbock D, Bowie AG: The history of Toll-like receptors - redefining innate immunity. Nat Rev Immunol 2013; 13:453-460.
    • (2013) Nat Rev Immunol , vol.13 , pp. 453-460
    • O'Neill, L.A.1    Golenbock, D.2    Bowie, A.G.3
  • 72
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated immune responses
    • Liew FY, Xu D, Brint E.K., O'Neill LA: Negative regulation of toll-like receptor-mediated immune responses. Nat Rev Immunol 2005; 5: 446-458.
    • (2005) Nat Rev Immunol , vol.5 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 73
    • 80052020185 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP acts as a negative regulator in inflammatory signaling triggered by toll-like receptors
    • Yuk JM, Shin DM, Lee H.M., Kim JJ, Kim SW, Jin HS, et al.: The orphan nuclear receptor SHP acts as a negative regulator in inflammatory signaling triggered by Toll-like receptors. Nat Immunol 2011; 12:742-751.
    • (2011) Nat Immunol , vol.12 , pp. 742-751
    • Yuk, J.M.1    Shin, D.M.2    Lee, H.M.3    Kim, J.J.4    Kim, S.W.5    Jin, H.S.6
  • 74
    • 0036006290 scopus 로고    scopus 로고
    • Regulation of Interleukin-1- and lipopolysac-charide-induced NF-kappaB activation by alternative splicing of MyD88
    • Janssens S, Burns K, Tschopp J., Beyaert R: Regulation of interleukin-1- and lipopolysac-charide-induced NF-kappaB activation by alternative splicing of MyD88. Curr Biol 2002; 12:467-471.
    • (2002) Curr Biol , vol.12 , pp. 467-471
    • Janssens, S.1    Burns, K.2    Tschopp, J.3    Beyaert, R.4
  • 75
    • 0042236366 scopus 로고    scopus 로고
    • MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression
    • Janssens S, Burns K, Vercammen E., Tschopp J, Beyaert R: MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression. FEBS Lett 2003; 548:103-107.
    • (2003) FEBS Lett , vol.548 , pp. 103-107
    • Janssens, S.1    Burns, K.2    Vercammen, E.3    Tschopp, J.4    Beyaert, R.5
  • 77
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent toll-like receptor signaling
    • Carty M, Goodbody R, Schroder M., Stack J, Moynagh PN, Bowie AG: The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nat Immunol 2006; 7:1074-1081.
    • (2006) Nat Immunol , vol.7 , pp. 1074-1081
    • Carty, M.1    Goodbody, R.2    Schroder, M.3    Stack, J.4    Moynagh, P.N.5    Bowie, A.G.6
  • 78
    • 84874230451 scopus 로고    scopus 로고
    • TRIF-mediated TLR3 and TLR4 signaling is negatively regulated by ADAM15
    • Ahmed S, Maratha A, Butt A.Q., Shevlin E., Miggin SM: TRIF-mediated TLR3 and TLR4 signaling is negatively regulated by ADAM15. J Immunol 2013; 190:2217-2228.
    • (2013) J Immunol , vol.190 , pp. 2217-2228
    • Ahmed, S.1    Maratha, A.2    Butt, A.Q.3    Shevlin, E.4    Miggin, S.M.5
  • 79
    • 84875549688 scopus 로고    scopus 로고
    • E3 ligase WWP2 negatively regulates TLR3-mediated innate immune response by targeting TRIF for ubiquitination and degradation
    • Yang Y, Liao B, Wang S., Yan B, Jin Y, Shu H.B., et al.: E3 ligase WWP2 negatively regulates TLR3-mediated innate immune response by targeting TRIF for ubiquitination and degradation. Proc Natl Acad Sci USA 2013; 110: 5115-5120.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 5115-5120
    • Yang, Y.1    Liao, B.2    Wang, S.3    Yan, B.4    Jin, Y.5    Shu, H.B.6
  • 80
    • 84867308377 scopus 로고    scopus 로고
    • TRIM38 negatively regulates TLR3-medi-ated IFN-β signaling by targeting TRIF for degradation
    • Xue Q, Zhou Z, Lei X., Liu X, He B, Wang J., et al.: TRIM38 negatively regulates TLR3-medi-ated IFN-β signaling by targeting TRIF for degradation. PLoS One 2012; 7:e46825.
    • (2012) PLoS One , vol.7
    • Xue, Q.1    Zhou, Z.2    Lei, X.3    Liu, X.4    He, B.5    Wang, J.6
  • 81
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on toll-like receptor 4
    • Shimazu R, Akashi S, Ogata H., Nagai Y, Fukudome K, Miyake K., et al.: MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 1999; 189:1777-1782.
    • (1999) J Exp Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6
  • 82
    • 77952377269 scopus 로고    scopus 로고
    • Negative regulation of MyD88-dependent signaling by IL-10 in dendritic cells
    • Chang J, Kunkel SL, Chang CH: Negative regulation of MyD88-dependent signaling by IL-10 in dendritic cells. Proc Natl Acad Sci USA 2009; 106:18327-18332.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18327-18332
    • Chang, J.1    Kunkel, S.L.2    Chang, C.H.3
  • 85
    • 20644450101 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor 4 signaling by the toll-like receptor homolog RP105
    • Divanovic S, Trompette A, Atabani S.F., Madan R., Golenbock DT, Visintin A, et al.: Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nat Immunol 2005; 6:571-578.
    • (2005) Nat Immunol , vol.6 , pp. 571-578
    • Divanovic, S.1    Trompette, A.2    Atabani, S.F.3    Madan, R.4    Golenbock, D.T.5    Visintin, A.6
  • 86
    • 84858122665 scopus 로고    scopus 로고
    • Role of G protein-coupled receptors in inflammation
    • Sun L, Ye RD: Role of G protein-coupled receptors in inflammation. Acta Pharmacol Sin 2012; 33:342-350.
    • (2012) Acta Pharmacol Sin , vol.33 , pp. 342-350
    • Sun, L.1    Ye, R.D.2
  • 87
    • 84857471063 scopus 로고    scopus 로고
    • Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins
    • Magalhaes AC, Dunn H, Ferguson SSG: Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins. Br J Pharmacol 2012; 165:1717-1736.
    • (2012) Br J Pharmacol , vol.165 , pp. 1717-1736
    • Magalhaes, A.C.1    Dunn, H.2    Ferguson, S.S.G.3
  • 88
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson SSG: Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 2001; 53:1-24.
    • (2001) Pharmacol Rev , vol.53 , pp. 1-24
    • Ferguson, S.S.G.1
  • 89
    • 18844464024 scopus 로고    scopus 로고
    • Control of aldosterone secretion: A model for convergence in cellular signaling pathways
    • Spat A, Hunyady L: Control of aldosterone secretion: a model for convergence in cellular signaling pathways. Physiol Rev 2004; 84:489-539.
    • (2004) Physiol Rev , vol.84 , pp. 489-539
    • Spat, A.1    Hunyady, L.2
  • 91
    • 23044455604 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor β (PDGFRβ)
    • Takayama Y, May P, Anderson RGW, Herz J: Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor β (PDGFRβ). J Biol Chem 2005; 280:18504-18510.
    • (2005) J Biol Chem , vol.280 , pp. 18504-18510
    • Takayama, Y.1    May, P.2    Anderson, R.G.W.3    Herz, J.4
  • 93
    • 30044449982 scopus 로고    scopus 로고
    • Resolution of inflammation: The beginning programs the end
    • Serhan CN, Savill J: Resolution of inflammation: the beginning programs the end. Nat Immunol 2005; 6:1191-1197.
    • (2005) Nat Immunol , vol.6 , pp. 1191-1197
    • Serhan, C.N.1    Savill, J.2
  • 94
    • 79955663260 scopus 로고    scopus 로고
    • The resolution of inflammation: The devil in the flask and in the details
    • Serhan CN: The resolution of inflammation: the devil in the flask and in the details. FASEB J 2011; 25:1441-1448.
    • (2011) FASEB J , vol.25 , pp. 1441-1448
    • Serhan, C.N.1
  • 95
    • 78549283981 scopus 로고    scopus 로고
    • Novel lipid mediators promote resolution of acute inflammation: Impact of aspirin and statins
    • Spite M, Serhan CN: Novel lipid mediators promote resolution of acute inflammation: impact of aspirin and statins. Circ Res 2010; 107:1170-1184.
    • (2010) Circ Res , vol.107 , pp. 1170-1184
    • Spite, M.1    Serhan, C.N.2
  • 96
    • 84866091918 scopus 로고    scopus 로고
    • Self-limited versus delayed resolution of acute inflammation: Temporal regulation of pro-resolving mediators and microRNA
    • Fredman G, Li Y, Dalli J., Chiang N, Serhan CN: Self-limited versus delayed resolution of acute inflammation: temporal regulation of pro-resolving mediators and microRNA. Sci Rep 2012; 2:639.
    • (2012) Sci Rep , vol.2 , pp. 639
    • Fredman, G.1    Li, Y.2    Dalli, J.3    Chiang, N.4    Serhan, C.N.5
  • 97
    • 58149094363 scopus 로고    scopus 로고
    • Annexin A1 and glucocorticoids as effectors of the resolution of inflammation
    • Perretti M, D'Acquisto F: Annexin A1 and glucocorticoids as effectors of the resolution of inflammation. Nat Rev Immunol 2009, 9: 62-70.
    • (2009) Nat Rev Immunol , vol.9 , pp. 62-70
    • Perretti, M.1    D'Acquisto, F.2
  • 98
    • 78649736380 scopus 로고    scopus 로고
    • The regulatory role of nitric oxide in proinflammatory cytokine expression during the induction and resolution of inflammation
    • Kobayashi Y: The regulatory role of nitric oxide in proinflammatory cytokine expression during the induction and resolution of inflammation. J Leukoc Biol 2010; 88:1157-1162.
    • (2010) J Leukoc Biol , vol.88 , pp. 1157-1162
    • Kobayashi, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.