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Volumn 584, Issue 24, 2010, Pages 4838-4844

CD46 signaling in T cells: Linking pathogens with polarity

Author keywords

CD46; Pathogens; Polarity; T cells

Indexed keywords

CELL PROTEIN; MEMBRANE COFACTOR PROTEIN; PROTEIN DLG; UNCLASSIFIED DRUG;

EID: 78649876882     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.09.003     Document Type: Review
Times cited : (11)

References (64)
  • 1
    • 0032057535 scopus 로고    scopus 로고
    • CD46 (membrane cofactor protein of complement, measles virus receptor): structural and functional divergence among species
    • Seya T., Nomura Y., Murakami N.A., Begum N.A., Matsumoto M., Nagasawa S. CD46 (membrane cofactor protein of complement, measles virus receptor): structural and functional divergence among species. Int. J. Mol. Med. 1998, 1:809-816.
    • (1998) Int. J. Mol. Med. , vol.1 , pp. 809-816
    • Seya, T.1    Nomura, Y.2    Murakami, N.A.3    Begum, N.A.4    Matsumoto, M.5    Nagasawa, S.6
  • 2
    • 0036176966 scopus 로고    scopus 로고
    • The murine complement regulator Crry: new insights into the immunobiology of complement regulation
    • Molina H. The murine complement regulator Crry: new insights into the immunobiology of complement regulation. Cell. Mol. Life Sci. 2002, 59:220-229.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 220-229
    • Molina, H.1
  • 3
    • 0025752408 scopus 로고
    • Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a regulator of complement activation
    • Purcell D.F., Russell S.M., Deacon N.J., Brown M.A., Hooker D.J., McKenzie I.F. Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a regulator of complement activation. Immunogenetics 1991, 33:335-344.
    • (1991) Immunogenetics , vol.33 , pp. 335-344
    • Purcell, D.F.1    Russell, S.M.2    Deacon, N.J.3    Brown, M.A.4    Hooker, D.J.5    McKenzie, I.F.6
  • 4
    • 32344435623 scopus 로고    scopus 로고
    • Holding T cells in check - a new role for complement regulators?
    • Longhi M.P., Harris C.L., Morgan B.P., Gallimore A. Holding T cells in check - a new role for complement regulators?. Trends Immunol. 2006, 27:102-108.
    • (2006) Trends Immunol. , vol.27 , pp. 102-108
    • Longhi, M.P.1    Harris, C.L.2    Morgan, B.P.3    Gallimore, A.4
  • 5
  • 6
    • 4644364097 scopus 로고    scopus 로고
    • Four viruses, two bacteria, and one receptor: membrane cofactor protein (CD46) as pathogens' magnet
    • Cattaneo R. Four viruses, two bacteria, and one receptor: membrane cofactor protein (CD46) as pathogens' magnet. J. Virol. 2004, 78:4385-4388.
    • (2004) J. Virol. , vol.78 , pp. 4385-4388
    • Cattaneo, R.1
  • 7
    • 0036569443 scopus 로고    scopus 로고
    • Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46)
    • Giannakis E., et al. Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46). J. Immunol. 2002, 168:4585-4592.
    • (2002) J. Immunol. , vol.168 , pp. 4585-4592
    • Giannakis, E.1
  • 8
    • 33750117119 scopus 로고    scopus 로고
    • Maintenance and modulation of T cell polarity
    • Krummel M.F., Macara I. Maintenance and modulation of T cell polarity. Nat. Immunol. 2006, 7:1143-1149.
    • (2006) Nat. Immunol. , vol.7 , pp. 1143-1149
    • Krummel, M.F.1    Macara, I.2
  • 9
    • 55849090253 scopus 로고    scopus 로고
    • Hunter to gatherer and back: immunological synapses and kinapses as variations on the theme of amoeboid locomotion
    • Dustin M.L. Hunter to gatherer and back: immunological synapses and kinapses as variations on the theme of amoeboid locomotion. Annu. Rev. Cell Dev. Biol. 2008, 24:577-596.
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 577-596
    • Dustin, M.L.1
  • 10
    • 0343953444 scopus 로고    scopus 로고
    • Cutting edge: CD46, a new costimulatory molecule for T cells, that induces p120CBL and LAT phosphorylation
    • Astier A., Trescol-Biemont M.C., Azocar O., Lamouille B., Rabourdin-Combe C. Cutting edge: CD46, a new costimulatory molecule for T cells, that induces p120CBL and LAT phosphorylation. J. Immunol. 2000, 164:6091-6095.
    • (2000) J. Immunol. , vol.164 , pp. 6091-6095
    • Astier, A.1    Trescol-Biemont, M.C.2    Azocar, O.3    Lamouille, B.4    Rabourdin-Combe, C.5
  • 11
    • 0034651964 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine phosphorylation
    • Wang G., Liszewski M.K., Chan A.C., Atkinson J.P. Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine phosphorylation. J. Immunol. 2000, 164:1839-1846.
    • (2000) J. Immunol. , vol.164 , pp. 1839-1846
    • Wang, G.1    Liszewski, M.K.2    Chan, A.C.3    Atkinson, J.P.4
  • 12
    • 4644363271 scopus 로고    scopus 로고
    • CD46-mediated costimulation induces a Th1-biased response and enhances early TCR/CD3 signaling in human CD4+ T lymphocytes
    • Sanchez A., Feito M.J., Rojo J.M. CD46-mediated costimulation induces a Th1-biased response and enhances early TCR/CD3 signaling in human CD4+ T lymphocytes. Eur. J. Immunol. 2004, 34:2439-2448.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2439-2448
    • Sanchez, A.1    Feito, M.J.2    Rojo, J.M.3
  • 13
    • 0035892881 scopus 로고    scopus 로고
    • CD46/CD3 costimulation induces morphological changes of human T cells and activation of Vav, Rac, and extracellular signal-regulated kinase mitogen-activated protein kinase
    • Zaffran Y., Destaing O., Roux A., Ory S., Nheu T., Jurdic P., Rabourdin-Combe C., Astier A.L. CD46/CD3 costimulation induces morphological changes of human T cells and activation of Vav, Rac, and extracellular signal-regulated kinase mitogen-activated protein kinase. J. Immunol. 2001, 167:6780-6785.
    • (2001) J. Immunol. , vol.167 , pp. 6780-6785
    • Zaffran, Y.1    Destaing, O.2    Roux, A.3    Ory, S.4    Nheu, T.5    Jurdic, P.6    Rabourdin-Combe, C.7    Astier, A.L.8
  • 15
    • 38949217682 scopus 로고    scopus 로고
    • How polarity shapes the destiny of T cells
    • Russell S. How polarity shapes the destiny of T cells. J. Cell Sci. 2008, 121:131-136.
    • (2008) J. Cell Sci. , vol.121 , pp. 131-136
    • Russell, S.1
  • 17
    • 33751347857 scopus 로고    scopus 로고
    • The Scribble and Par complexes in polarity and migration: friends or foes?
    • Humbert P.O., Dow L.E., Russell S.M. The Scribble and Par complexes in polarity and migration: friends or foes?. Trends Cell Biol. 2006, 16:622-630.
    • (2006) Trends Cell Biol. , vol.16 , pp. 622-630
    • Humbert, P.O.1    Dow, L.E.2    Russell, S.M.3
  • 18
    • 77954886643 scopus 로고    scopus 로고
    • Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse
    • Lasserre R., et al. Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse. EMBO J. 2010, 29:2301-2314.
    • (2010) EMBO J. , vol.29 , pp. 2301-2314
    • Lasserre, R.1
  • 20
    • 20444445916 scopus 로고    scopus 로고
    • A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation
    • Ludford-Menting M.J., et al. A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation. Immunity 2005, 22:737-748.
    • (2005) Immunity , vol.22 , pp. 737-748
    • Ludford-Menting, M.J.1
  • 21
    • 24944577909 scopus 로고    scopus 로고
    • Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization
    • Etienne-Manneville S., Manneville J.B., Nicholls S., Ferenczi M.A., Hall A. Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization. J. Cell Biol. 2005, 170:895-901.
    • (2005) J. Cell Biol. , vol.170 , pp. 895-901
    • Etienne-Manneville, S.1    Manneville, J.B.2    Nicholls, S.3    Ferenczi, M.A.4    Hall, A.5
  • 22
    • 22244455455 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions
    • Funke L., Dakoji S., Bredt D.S. Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions. Annu. Rev. Biochem. 2005, 74:219-245.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 219-245
    • Funke, L.1    Dakoji, S.2    Bredt, D.S.3
  • 23
    • 4444382955 scopus 로고    scopus 로고
    • Discs large (Dlg1) complexes in lymphocyte activation
    • Xavier R., et al. Discs large (Dlg1) complexes in lymphocyte activation. J. Cell Biol. 2004, 166:173-178.
    • (2004) J. Cell Biol. , vol.166 , pp. 173-178
    • Xavier, R.1
  • 24
    • 4043099715 scopus 로고    scopus 로고
    • The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large
    • Ralston K.J., et al. The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large. J. Biol. Chem. 2004, 279:33816-33828.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33816-33828
    • Ralston, K.J.1
  • 25
    • 33846514807 scopus 로고    scopus 로고
    • Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors
    • Round J.L., Humphries L.A., Tomassian T., Mittelstadt P., Zhang M., Miceli M.C. Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors. Nat. Immunol. 2007, 8:154-161.
    • (2007) Nat. Immunol. , vol.8 , pp. 154-161
    • Round, J.L.1    Humphries, L.A.2    Tomassian, T.3    Mittelstadt, P.4    Zhang, M.5    Miceli, M.C.6
  • 26
    • 13644268540 scopus 로고    scopus 로고
    • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells
    • Round J.L., Tomassian T., Zhang M., Patel V., Schoenberger S.P., Miceli M.C. Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. J. Exp. Med. 2005, 201:419-430.
    • (2005) J. Exp. Med. , vol.201 , pp. 419-430
    • Round, J.L.1    Tomassian, T.2    Zhang, M.3    Patel, V.4    Schoenberger, S.P.5    Miceli, M.C.6
  • 27
    • 0036305568 scopus 로고    scopus 로고
    • Linking innate and acquired immunity: divergent role of CD46 cytoplasmic domains in T cell induced inflammation
    • Marie J.C., Astier A.L., Rivailler P., Rabourdin-Combe C., Wild T.F., Horvat B. Linking innate and acquired immunity: divergent role of CD46 cytoplasmic domains in T cell induced inflammation. Nat. Immunol. 2002, 3:659-666.
    • (2002) Nat. Immunol. , vol.3 , pp. 659-666
    • Marie, J.C.1    Astier, A.L.2    Rivailler, P.3    Rabourdin-Combe, C.4    Wild, T.F.5    Horvat, B.6
  • 28
    • 77949888199 scopus 로고    scopus 로고
    • Plasma membrane rafts engaged in T cell signalling: new developments in an old concept
    • Harder T., Sangani D. Plasma membrane rafts engaged in T cell signalling: new developments in an old concept. Cell Commun. Signal 2009, 7:21.
    • (2009) Cell Commun. Signal , vol.7 , pp. 21
    • Harder, T.1    Sangani, D.2
  • 29
    • 33645075194 scopus 로고    scopus 로고
    • Compartmentalization in T-cell signalling: membrane microdomains and polarity orchestrate signalling and morphology
    • Russell S., Oliaro J. Compartmentalization in T-cell signalling: membrane microdomains and polarity orchestrate signalling and morphology. Immunol. Cell Biol. 2006, 84:107-113.
    • (2006) Immunol. Cell Biol. , vol.84 , pp. 107-113
    • Russell, S.1    Oliaro, J.2
  • 30
    • 26444452661 scopus 로고    scopus 로고
    • Condensation of the plasma membrane at the site of T lymphocyte activation
    • Gaus K., Chklovskaia E., Jessup B., Jessup W., Harder T. Condensation of the plasma membrane at the site of T lymphocyte activation. J. Cell Biol. 2005, 171:121-131.
    • (2005) J. Cell Biol. , vol.171 , pp. 121-131
    • Gaus, K.1    Chklovskaia, E.2    Jessup, B.3    Jessup, W.4    Harder, T.5
  • 31
    • 48249088456 scopus 로고    scopus 로고
    • Functional implications of plasma membrane condensation for T cell activation
    • Rentero C., et al. Functional implications of plasma membrane condensation for T cell activation. PLoS ONE 2008, 3:e2262.
    • (2008) PLoS ONE , vol.3
    • Rentero, C.1
  • 32
    • 49049088092 scopus 로고    scopus 로고
    • Human herpesvirus-6 infection induces the reorganization of membrane microdomains in target cells, which are required for virus entry
    • Tang H., Kawabata A., Takemoto M., Yamanishi K., Mori Y. Human herpesvirus-6 infection induces the reorganization of membrane microdomains in target cells, which are required for virus entry. Virology 2008, 378:265-271.
    • (2008) Virology , vol.378 , pp. 265-271
    • Tang, H.1    Kawabata, A.2    Takemoto, M.3    Yamanishi, K.4    Mori, Y.5
  • 33
    • 0034666131 scopus 로고    scopus 로고
    • GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes
    • Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H. GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes. J. Biol. Chem. 2000, 275:28774-28784.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28774-28784
    • Hanada, T.1    Lin, L.2    Tibaldi, E.V.3    Reinherz, E.L.4    Chishti, A.H.5
  • 34
    • 65649098764 scopus 로고    scopus 로고
    • The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells
    • Kaizuka Y., Douglass A.D., Vardhana S., Dustin M.L., Vale R.D. The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells. J. Cell Biol. 2009, 185:521-534.
    • (2009) J. Cell Biol. , vol.185 , pp. 521-534
    • Kaizuka, Y.1    Douglass, A.D.2    Vardhana, S.3    Dustin, M.L.4    Vale, R.D.5
  • 35
    • 0347895101 scopus 로고    scopus 로고
    • Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype
    • Kemper C., Chan A.C., Green J.M., Brett K.A., Murphy K.M., Atkinson J.P. Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype. Nature 2003, 421:388-392.
    • (2003) Nature , vol.421 , pp. 388-392
    • Kemper, C.1    Chan, A.C.2    Green, J.M.3    Brett, K.A.4    Murphy, K.M.5    Atkinson, J.P.6
  • 36
    • 77956201049 scopus 로고    scopus 로고
    • Asymmetric cell division of T cells upon antigen presentation uses multiple conserved mechanisms
    • Oliaro J., et al. Asymmetric cell division of T cells upon antigen presentation uses multiple conserved mechanisms. J Immunol 2010, 185:367-375.
    • (2010) J Immunol , vol.185 , pp. 367-375
    • Oliaro, J.1
  • 37
    • 33947730608 scopus 로고    scopus 로고
    • Asymmetric T lymphocyte division in the initiation of adaptive immune responses
    • Chang J.T., et al. Asymmetric T lymphocyte division in the initiation of adaptive immune responses. Science 2007, 315:1687-1691.
    • (2007) Science , vol.315 , pp. 1687-1691
    • Chang, J.T.1
  • 38
    • 39149130360 scopus 로고    scopus 로고
    • Mechanisms of asymmetric stem cell division
    • Knoblich J.A. Mechanisms of asymmetric stem cell division. Cell 2008, 132:583-597.
    • (2008) Cell , vol.132 , pp. 583-597
    • Knoblich, J.A.1
  • 39
    • 73349089365 scopus 로고    scopus 로고
    • Global reductions in measles mortality 2000-2008 and the risk of measles resurgence
    • WHO
    • Global reductions in measles mortality 2000-2008 and the risk of measles resurgence. Weekly Epidemiological Report 2009, 84:505-516. WHO.
    • (2009) Weekly Epidemiological Report , vol.84 , pp. 505-516
  • 40
    • 45749114494 scopus 로고    scopus 로고
    • Receptor interactions, tropism, and mechanisms involved in morbillivirus-induced immunomodulation
    • Schneider-Schaulies J., Schneider-Schaulies S. Receptor interactions, tropism, and mechanisms involved in morbillivirus-induced immunomodulation. Adv. Virus Res. 2008, 71:173-205.
    • (2008) Adv. Virus Res. , vol.71 , pp. 173-205
    • Schneider-Schaulies, J.1    Schneider-Schaulies, S.2
  • 41
    • 31144434938 scopus 로고    scopus 로고
    • Immunosuppression caused by measles virus: role of viral proteins
    • Kerdiles Y.M., Sellin C.I., Druelle J., Horvat B. Immunosuppression caused by measles virus: role of viral proteins. Rev. Med. Virol. 2006, 16:49-63.
    • (2006) Rev. Med. Virol. , vol.16 , pp. 49-63
    • Kerdiles, Y.M.1    Sellin, C.I.2    Druelle, J.3    Horvat, B.4
  • 42
    • 4143074753 scopus 로고    scopus 로고
    • Measles virus interacts with and alters signal transduction in T-cell lipid rafts
    • Avota E., Muller N., Klett M., Schneider-Schaulies S. Measles virus interacts with and alters signal transduction in T-cell lipid rafts. J. Virol. 2004, 78:9552-9559.
    • (2004) J. Virol. , vol.78 , pp. 9552-9559
    • Avota, E.1    Muller, N.2    Klett, M.3    Schneider-Schaulies, S.4
  • 43
    • 33745034465 scopus 로고    scopus 로고
    • Measles virus contact with T cells impedes cytoskeletal remodeling associated with spreading, polarization, and CD3 clustering
    • Muller N., Avota E., Schneider-Schaulies J., Harms H., Krohne G., Schneider-Schaulies S. Measles virus contact with T cells impedes cytoskeletal remodeling associated with spreading, polarization, and CD3 clustering. Traffic 2006, 7:849-858.
    • (2006) Traffic , vol.7 , pp. 849-858
    • Muller, N.1    Avota, E.2    Schneider-Schaulies, J.3    Harms, H.4    Krohne, G.5    Schneider-Schaulies, S.6
  • 45
    • 0036009113 scopus 로고    scopus 로고
    • Neisserial binding to CEACAM1 arrests the activation and proliferation of CD4+ T lymphocytes
    • Boulton I.C., Gray-Owen S.D. Neisserial binding to CEACAM1 arrests the activation and proliferation of CD4+ T lymphocytes. Nat. Immunol. 2002, 3:229-236.
    • (2002) Nat. Immunol. , vol.3 , pp. 229-236
    • Boulton, I.C.1    Gray-Owen, S.D.2
  • 46
    • 0030864090 scopus 로고    scopus 로고
    • Attachment of piliated, Opa- and Opc- gonococci and meningococci to epithelial cells elicits cortical actin rearrangements and clustering of tyrosine-phosphorylated proteins
    • Merz A.J., So M. Attachment of piliated, Opa- and Opc- gonococci and meningococci to epithelial cells elicits cortical actin rearrangements and clustering of tyrosine-phosphorylated proteins. Infect. Immun. 1997, 65:4341-4349.
    • (1997) Infect. Immun. , vol.65 , pp. 4341-4349
    • Merz, A.J.1    So, M.2
  • 47
    • 23844439242 scopus 로고    scopus 로고
    • PilT is required for PI(3, 4, 5)P3-mediated crosstalk between Neisseria gonorrhoeae and epithelial cells
    • Lee S.W., Higashi D.L., Snyder A., Merz A.J., Potter L., So M. PilT is required for PI(3, 4, 5)P3-mediated crosstalk between Neisseria gonorrhoeae and epithelial cells. Cell. Microbiol. 2005, 7:1271-1284.
    • (2005) Cell. Microbiol. , vol.7 , pp. 1271-1284
    • Lee, S.W.1    Higashi, D.L.2    Snyder, A.3    Merz, A.J.4    Potter, L.5    So, M.6
  • 48
    • 0030779080 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
    • Kallstrom H., Liszewski M.K., Atkinson J.P., Jonsson A.B. Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria. Mol. Microbiol. 1997, 25:639-647.
    • (1997) Mol. Microbiol. , vol.25 , pp. 639-647
    • Kallstrom, H.1    Liszewski, M.K.2    Atkinson, J.P.3    Jonsson, A.B.4
  • 49
    • 33645519608 scopus 로고    scopus 로고
    • Monoclonal antibody detection of CD46 clustering beneath Neisseria gonorrhoeae microcolonies
    • Weyand N.J., Lee S.W., Higashi D.L., Cawley D., Yoshihara P., So M. Monoclonal antibody detection of CD46 clustering beneath Neisseria gonorrhoeae microcolonies. Infect. Immun. 2006, 74:2428-2435.
    • (2006) Infect. Immun. , vol.74 , pp. 2428-2435
    • Weyand, N.J.1    Lee, S.W.2    Higashi, D.L.3    Cawley, D.4    Yoshihara, P.5    So, M.6
  • 50
    • 0029846832 scopus 로고    scopus 로고
    • Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain
    • Lue R.A., Brandin E., Chan E.P., Branton D. Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. J. Cell Biol. 1996, 135:1125-1137.
    • (1996) J. Cell Biol. , vol.135 , pp. 1125-1137
    • Lue, R.A.1    Brandin, E.2    Chan, E.P.3    Branton, D.4
  • 51
    • 23244448609 scopus 로고    scopus 로고
    • Induction of a regulatory phenotype in human CD4+ T cells by streptococcal M protein
    • Price J.D., Schaumburg J., Sandin C., Atkinson J.P., Lindahl G., Kemper C. Induction of a regulatory phenotype in human CD4+ T cells by streptococcal M protein. J. Immunol. 2005, 175:677-684.
    • (2005) J. Immunol. , vol.175 , pp. 677-684
    • Price, J.D.1    Schaumburg, J.2    Sandin, C.3    Atkinson, J.P.4    Lindahl, G.5    Kemper, C.6
  • 52
    • 73849090193 scopus 로고    scopus 로고
    • Complement and its role in innate and adaptive immune responses
    • Dunkelberger J.R., Song W.C. Complement and its role in innate and adaptive immune responses. Cell Res. 2010, 20:34-50.
    • (2010) Cell Res. , vol.20 , pp. 34-50
    • Dunkelberger, J.R.1    Song, W.C.2
  • 53
    • 33845905781 scopus 로고    scopus 로고
    • T-cell regulation: with complements from innate immunity
    • Kemper C., Atkinson J.P. T-cell regulation: with complements from innate immunity. Nat. Rev. Immunol. 2007, 7:9-18.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 9-18
    • Kemper, C.1    Atkinson, J.P.2
  • 56
    • 3242800341 scopus 로고    scopus 로고
    • CD46: a complement regulator and pathogen receptor that mediates links between innate and acquired immune function
    • Russell S. CD46: a complement regulator and pathogen receptor that mediates links between innate and acquired immune function. Tissue Antigens 2004, 64:111-118.
    • (2004) Tissue Antigens , vol.64 , pp. 111-118
    • Russell, S.1
  • 57
    • 0033559981 scopus 로고    scopus 로고
    • Transgenic interleukin 10 prevents induction of experimental autoimmune encephalomyelitis
    • Cua D.J., Groux H., Hinton D.R., Stohlman S.A., Coffman R.L. Transgenic interleukin 10 prevents induction of experimental autoimmune encephalomyelitis. J. Exp. Med. 1999, 189:1005-1010.
    • (1999) J. Exp. Med. , vol.189 , pp. 1005-1010
    • Cua, D.J.1    Groux, H.2    Hinton, D.R.3    Stohlman, S.A.4    Coffman, R.L.5
  • 58
    • 35848964590 scopus 로고    scopus 로고
    • Abnormal Tr1 differentiation in multiple sclerosis
    • Astier A.L., Hafler D.A. Abnormal Tr1 differentiation in multiple sclerosis. J. Neuroimmunol. 2007, 191:70-78.
    • (2007) J. Neuroimmunol. , vol.191 , pp. 70-78
    • Astier, A.L.1    Hafler, D.A.2
  • 59
    • 33845302957 scopus 로고    scopus 로고
    • Alterations in CD46-mediated Tr1 regulatory T cells in patients with multiple sclerosis
    • Astier A.L., Meiffren G., Freeman S., Hafler D.A. Alterations in CD46-mediated Tr1 regulatory T cells in patients with multiple sclerosis. J. Clin. Invest. 2006, 116:3252-3257.
    • (2006) J. Clin. Invest. , vol.116 , pp. 3252-3257
    • Astier, A.L.1    Meiffren, G.2    Freeman, S.3    Hafler, D.A.4
  • 60
    • 0036295091 scopus 로고    scopus 로고
    • Subtractive expression cloning reveals high expression of CD46 at the blood-brain barrier
    • Shusta E.V., Zhu C., Boado R.J., Pardridge W.M. Subtractive expression cloning reveals high expression of CD46 at the blood-brain barrier. J. Neuropathol. Exp. Neurol. 2002, 61:597-604.
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 597-604
    • Shusta, E.V.1    Zhu, C.2    Boado, R.J.3    Pardridge, W.M.4
  • 62
    • 0041563779 scopus 로고    scopus 로고
    • Obstacles to cancer immunotherapy: expression of membrane complement regulatory proteins (mCRPs) in tumors
    • Fishelson Z., Donin N., Zell S., Schultz S., Kirschfink M. Obstacles to cancer immunotherapy: expression of membrane complement regulatory proteins (mCRPs) in tumors. Mol. Immunol. 2003, 40:109-123.
    • (2003) Mol. Immunol. , vol.40 , pp. 109-123
    • Fishelson, Z.1    Donin, N.2    Zell, S.3    Schultz, S.4    Kirschfink, M.5
  • 63
    • 14844331708 scopus 로고    scopus 로고
    • Measles as a potential oncolytic virus
    • Fielding A.K. Measles as a potential oncolytic virus. Rev. Med. Virol. 2005, 15:135-142.
    • (2005) Rev. Med. Virol. , vol.15 , pp. 135-142
    • Fielding, A.K.1
  • 64
    • 23044480130 scopus 로고    scopus 로고
    • Engagement of specific T-cell surface molecules regulates cytoskeletal polarization in HTLV-1-infected lymphocytes
    • Barnard A.L., Igakura T., Tanaka Y., Taylor G.P., Bangham C.R. Engagement of specific T-cell surface molecules regulates cytoskeletal polarization in HTLV-1-infected lymphocytes. Blood 2005, 106:988-995.
    • (2005) Blood , vol.106 , pp. 988-995
    • Barnard, A.L.1    Igakura, T.2    Tanaka, Y.3    Taylor, G.P.4    Bangham, C.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.