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Volumn 113, Issue 40, 2016, Pages E5944-E5951

Optimal activation of Fc-mediated effector functions by influenza virus hemagglutinin antibodies requires two points of contact

Author keywords

Antibody dependent cell mediated immunity; Broadly reactive antibodies; Fc receptor; Hemagglutinin; Influenza virus

Indexed keywords

EPITOPE; FC RECEPTOR; IMMUNOGLOBULIN F(AB) FRAGMENT; INFLUENZA VIRUS HEMAGGLUTININ; MONOCLONAL ANTIBODY; SIALIC ACID; N ACETYLNEURAMINIC ACID; VIRUS ANTIBODY;

EID: 84989895227     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1613225113     Document Type: Article
Times cited : (101)

References (57)
  • 1
    • 84911427961 scopus 로고    scopus 로고
    • Accessed September 9, 2016
    • World Health Organization (2014) Fact Sheet 211: Influenza. Available at: www.who.int/mediacentre/factsheets/fs211/en/. Accessed September 9, 2016.
    • (2014) Fact Sheet 211: Influenza
  • 2
    • 84921503793 scopus 로고    scopus 로고
    • Advances in universal influenza virus vaccine design and antibody-mediated therapies based on conserved regions of the hemagglutinin
    • Krammer F, Palese P, Steel J (2014) Advances in universal influenza virus vaccine design and antibody-mediated therapies based on conserved regions of the hemagglutinin. Curr Top Microbiol Immunol 386:301-321.
    • (2014) Curr Top Microbiol Immunol , vol.386 , pp. 301-321
    • Krammer, F.1    Palese, P.2    Steel, J.3
  • 3
    • 51449086295 scopus 로고    scopus 로고
    • The biology of influenza viruses
    • Bouvier NM, Palese P (2008) The biology of influenza viruses. Vaccine 26(Suppl 4):D49-D53.
    • (2008) Vaccine , vol.26 , pp. D49-D53
    • Bouvier, N.M.1    Palese, P.2
  • 4
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviruses
    • eds Knipe DM, Howley PM (Lippincott-Raven, Philadelphia, PA), 4th Ed
    • Shaw ML, Palese P (2007) Orthomyxoviruses. Fields Virology, eds Knipe DM, Howley PM (Lippincott-Raven, Philadelphia, PA), 4th Ed.
    • (2007) Fields Virology
    • Shaw, M.L.1    Palese, P.2
  • 5
    • 0015452705 scopus 로고
    • The role of serum haemagglutination-inhibiting antibody in protection against challenge infection with influenza A2 and B viruses
    • Hobson D, Curry RL, Beare AS, Ward-Gardner A (1972) The role of serum haemagglutination-inhibiting antibody in protection against challenge infection with influenza A2 and B viruses. J Hyg (Lond) 70(4):767-777.
    • (1972) J Hyg (Lond) , vol.70 , Issue.4 , pp. 767-777
    • Hobson, D.1    Curry, R.L.2    Beare, A.S.3    Ward-Gardner, A.4
  • 6
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno Y, Isegawa Y, Sasao F, Ueda S (1993) A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J Virol 67(5):2552-2558.
    • (1993) J Virol , vol.67 , Issue.5 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 7
    • 84863597077 scopus 로고    scopus 로고
    • A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo
    • Tan GS, et al. (2012) A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo. J Virol 86(11):6179-6188.
    • (2012) J Virol , vol.86 , Issue.11 , pp. 6179-6188
    • Tan, G.S.1
  • 8
    • 84911434712 scopus 로고    scopus 로고
    • Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin
    • Tan GS, et al. (2014) Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin. J Virol 88(23):13580-13592.
    • (2014) J Virol , vol.88 , Issue.23 , pp. 13580-13592
    • Tan, G.S.1
  • 9
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert DC, et al. (2009) Antibody recognition of a highly conserved influenza virus epitope. Science 324(5924):246-251.
    • (2009) Science , vol.324 , Issue.5924 , pp. 246-251
    • Ekiert, D.C.1
  • 10
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert DC, et al. (2011) A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333(6044):843-850.
    • (2011) Science , vol.333 , Issue.6044 , pp. 843-850
    • Ekiert, D.C.1
  • 11
    • 84891910969 scopus 로고    scopus 로고
    • A common solution to group 2 influenza virus neutralization
    • Friesen RHE, et al. (2014) A common solution to group 2 influenza virus neutralization. Proc Natl Acad Sci USA 111(1):445-450.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.1 , pp. 445-450
    • Friesen, R.H.E.1
  • 12
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus C, et al. (2012) Highly conserved protective epitopes on influenza B viruses. Science 337(6100):1343-1348.
    • (2012) Science , vol.337 , Issue.6100 , pp. 1343-1348
    • Dreyfus, C.1
  • 13
    • 77649242815 scopus 로고    scopus 로고
    • Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins
    • Wang TT, et al. (2010) Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins. PLoS Pathog 6(2):e1000796.
    • (2010) PLoS Pathog , vol.6 , Issue.2
    • Wang, T.T.1
  • 14
    • 84878611784 scopus 로고    scopus 로고
    • Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies
    • Krammer F, Pica N, Hai R, Margine I, Palese P (2013) Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies. J Virol 87(12):6542-6550.
    • (2013) J Virol , vol.87 , Issue.12 , pp. 6542-6550
    • Krammer, F.1    Pica, N.2    Hai, R.3    Margine, I.4    Palese, P.5
  • 15
    • 84941023600 scopus 로고    scopus 로고
    • Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
    • Yassine HM, et al. (2015) Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection. Nat Med 21(9):1065-1070.
    • (2015) Nat Med , vol.21 , Issue.9 , pp. 1065-1070
    • Yassine, H.M.1
  • 16
    • 79952140653 scopus 로고    scopus 로고
    • Influenza virus vaccine based on the conserved hemagglutinin stalk domain
    • Steel J, et al. (2010) Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 1(1):e00018-10.
    • (2010) MBio , vol.1 , Issue.1 , pp. e00018-e00110
    • Steel, J.1
  • 17
    • 84941873935 scopus 로고    scopus 로고
    • A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
    • Impagliazzo A, et al. (2015) A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen. Science 349(6254):1301-1306.
    • (2015) Science , vol.349 , Issue.6254 , pp. 1301-1306
    • Impagliazzo, A.1
  • 18
    • 84931573106 scopus 로고    scopus 로고
    • Vaccination with soluble headless hemagglutinin protects mice from challenge with divergent influenza viruses
    • Wohlbold TJ, et al. (2015) Vaccination with soluble headless hemagglutinin protects mice from challenge with divergent influenza viruses. Vaccine 33(29):3314-3321.
    • (2015) Vaccine , vol.33 , Issue.29 , pp. 3314-3321
    • Wohlbold, T.J.1
  • 19
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo
    • DiLillo DJ, Tan GS, Palese P, Ravetch JV (2014) Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo. Nat Med 20(2):143-151.
    • (2014) Nat Med , vol.20 , Issue.2 , pp. 143-151
    • DiLillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 20
    • 84924777947 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza virus antibodies: Enhancement of neutralizing potency in polyclonal mixtures and IgA backbones
    • He W, et al. (2015) Broadly neutralizing anti-influenza virus antibodies: Enhancement of neutralizing potency in polyclonal mixtures and IgA backbones. J Virol 89(7):3610-3618.
    • (2015) J Virol , vol.89 , Issue.7 , pp. 3610-3618
    • He, W.1
  • 21
    • 84956934982 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
    • DiLillo DJ, Palese P, Wilson PC, Ravetch JV (2016) Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J Clin Invest 126(2):605-610.
    • (2016) J Clin Invest , vol.126 , Issue.2 , pp. 605-610
    • DiLillo, D.J.1    Palese, P.2    Wilson, P.C.3    Ravetch, J.V.4
  • 22
    • 84930822871 scopus 로고    scopus 로고
    • FcγR-dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities
    • Nimmerjahn F, Gordan S, Lux A (2015) FcγR-dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities. Trends Immunol 36(6):325-336.
    • (2015) Trends Immunol , vol.36 , Issue.6 , pp. 325-336
    • Nimmerjahn, F.1    Gordan, S.2    Lux, A.3
  • 23
    • 27644529984 scopus 로고    scopus 로고
    • Natural cytotoxicity receptors: Pattern recognition and involvement of carbohydrates
    • Porgador A (2005) Natural cytotoxicity receptors: Pattern recognition and involvement of carbohydrates. ScientificWorldJournal 5:151-154.
    • (2005) ScientificWorldJournal , vol.5 , pp. 151-154
    • Porgador, A.1
  • 24
    • 0035059950 scopus 로고    scopus 로고
    • Activating receptors and coreceptors involved in human natural killer cell-mediated cytolysis
    • Moretta A, et al. (2001) Activating receptors and coreceptors involved in human natural killer cell-mediated cytolysis. Annu Rev Immunol 19:197-223.
    • (2001) Annu Rev Immunol , vol.19 , pp. 197-223
    • Moretta, A.1
  • 25
  • 26
    • 84977126665 scopus 로고    scopus 로고
    • The role of Fc gamma receptors in the activity of immunomodulatory antibodies for cancer
    • Stewart R, Hammond SA, Oberst M, Wilkinson RW (2014) The role of Fc gamma receptors in the activity of immunomodulatory antibodies for cancer. J Immunother Cancer 2:29.
    • (2014) J Immunother Cancer , vol.2 , pp. 29
    • Stewart, R.1    Hammond, S.A.2    Oberst, M.3    Wilkinson, R.W.4
  • 27
    • 30444461383 scopus 로고    scopus 로고
    • Fcgamma receptors: Old friends and new family members
    • Nimmerjahn F, Ravetch JV (2006) Fcgamma receptors: Old friends and new family members. Immunity 24(1):19-28.
    • (2006) Immunity , vol.24 , Issue.1 , pp. 19-28
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 28
    • 35548955496 scopus 로고    scopus 로고
    • Fc-receptors as regulators of immunity
    • Nimmerjahn F, Ravetch JV (2007) Fc-receptors as regulators of immunity. Adv Immunol 96:179-204.
    • (2007) Adv Immunol , vol.96 , pp. 179-204
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 29
    • 84961938333 scopus 로고    scopus 로고
    • Fc-receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions
    • DiLillo DJ, Ravetch JV (2015) Fc-receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions. Cancer Immunol Res 3(7):704-713.
    • (2015) Cancer Immunol Res , vol.3 , Issue.7 , pp. 704-713
    • DiLillo, D.J.1    Ravetch, J.V.2
  • 30
    • 84890281675 scopus 로고    scopus 로고
    • Genome-wide mutagenesis of influenza virus reveals unique plasticity of the hemagglutinin and NS1 proteins
    • Heaton NS, Sachs D, Chen CJ (2013) Genome-wide mutagenesis of influenza virus reveals unique plasticity of the hemagglutinin and NS1 proteins. Proc Natl Acad Sci USA 110(50):20248-20253.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.50 , pp. 20248-20253
    • Heaton, N.S.1    Sachs, D.2    Chen, C.J.3
  • 31
    • 0022492323 scopus 로고
    • Characterization of monoclonal antibodies specific for sequential influenza A/PR/8/34 virus variants
    • Reale MA, et al. (1986) Characterization of monoclonal antibodies specific for sequential influenza A/PR/8/34 virus variants. J Immunol 137(4):1352-1358.
    • (1986) J Immunol , vol.137 , Issue.4 , pp. 1352-1358
    • Reale, M.A.1
  • 32
    • 22544487815 scopus 로고    scopus 로고
    • FcgammaRIV: A novel FcR with distinct IgG subclass specificity
    • Nimmerjahn F, Bruhns P, Horiuchi K, Ravetch JV (2005) FcgammaRIV: A novel FcR with distinct IgG subclass specificity. Immunity 23(1):41-51.
    • (2005) Immunity , vol.23 , Issue.1 , pp. 41-51
    • Nimmerjahn, F.1    Bruhns, P.2    Horiuchi, K.3    Ravetch, J.V.4
  • 33
    • 84965127880 scopus 로고    scopus 로고
    • Cryo-electron microscopy structures of chimeric hemagglutinin displayed on a universal influenza vaccine candidate
    • Tran EEH, et al. (2016) Cryo-electron microscopy structures of chimeric hemagglutinin displayed on a universal influenza vaccine candidate. MBio 7(2):e00257.
    • (2016) MBio , vol.7 , Issue.2
    • Tran, E.E.H.1
  • 34
    • 84896917279 scopus 로고    scopus 로고
    • Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages
    • Whittle JRR, et al. (2014) Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages. J Virol 88(8):4047-4057.
    • (2014) J Virol , vol.88 , Issue.8 , pp. 4047-4057
    • Whittle, J.R.R.1
  • 35
    • 0032005708 scopus 로고    scopus 로고
    • Studies of the binding properties of influenza hemagglutinin receptor-site mutants
    • Martín J, et al. (1998) Studies of the binding properties of influenza hemagglutinin receptor-site mutants. Virology 241(1):101-111.
    • (1998) Virology , vol.241 , Issue.1 , pp. 101-111
    • Martín, J.1
  • 36
    • 0035931861 scopus 로고    scopus 로고
    • Recognition of haemagglutinins on virus-infected cells by NKp46 activates lysis by human NK cells
    • Mandelboim O, et al. (2001) Recognition of haemagglutinins on virus-infected cells by NKp46 activates lysis by human NK cells. Nature 409(6823):1055-1060.
    • (2001) Nature , vol.409 , Issue.6823 , pp. 1055-1060
    • Mandelboim, O.1
  • 37
    • 80052318719 scopus 로고    scopus 로고
    • Modulation of NKp30- and NKp46-mediated natural killer cell responses by poxviral hemagglutinin
    • Jarahian M, et al. (2011) Modulation of NKp30- and NKp46-mediated natural killer cell responses by poxviral hemagglutinin. PLoS Pathog 7(8):e1002195.
    • (2011) PLoS Pathog , vol.7 , Issue.8
    • Jarahian, M.1
  • 38
    • 0034801637 scopus 로고    scopus 로고
    • Recognition of viral hemagglutinins by NKp44 but not by NKp30
    • Arnon TI, et al. (2001) Recognition of viral hemagglutinins by NKp44 but not by NKp30. Eur J Immunol 31(9):2680-2689.
    • (2001) Eur J Immunol , vol.31 , Issue.9 , pp. 2680-2689
    • Arnon, T.I.1
  • 39
    • 33645964977 scopus 로고    scopus 로고
    • Lethal influenza infection in the absence of the natural killer cell receptor gene Ncr1
    • Gazit R, et al. (2006) Lethal influenza infection in the absence of the natural killer cell receptor gene Ncr1. Nat Immunol 7(5):517-523.
    • (2006) Nat Immunol , vol.7 , Issue.5 , pp. 517-523
    • Gazit, R.1
  • 40
    • 67749124472 scopus 로고    scopus 로고
    • Activation of natural killer cells by newcastle disease virus hemagglutinin-neuraminidase
    • Jarahian M, et al. (2009) Activation of natural killer cells by newcastle disease virus hemagglutinin-neuraminidase. J Virol 83(16):8108-8121.
    • (2009) J Virol , vol.83 , Issue.16 , pp. 8108-8121
    • Jarahian, M.1
  • 41
    • 34047232835 scopus 로고    scopus 로고
    • Expression of ICP0 is sufficient to trigger natural killer cell recognition of herpes simplex virus-infected cells by natural cytotoxicity receptors
    • Chisholm SE, Howard K, Gómez MV, Reyburn HT (2007) Expression of ICP0 is sufficient to trigger natural killer cell recognition of herpes simplex virus-infected cells by natural cytotoxicity receptors. J Infect Dis 195(8):1160-1168.
    • (2007) J Infect Dis , vol.195 , Issue.8 , pp. 1160-1168
    • Chisholm, S.E.1    Howard, K.2    Gómez, M.V.3    Reyburn, H.T.4
  • 42
    • 23344448979 scopus 로고    scopus 로고
    • + T cells during HIV-1 infection: A gp41 peptide induces the expression of an NKp44 ligand
    • + T cells during HIV-1 infection: A gp41 peptide induces the expression of an NKp44 ligand. Proc Natl Acad Sci USA 102(31):10981-10986.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.31 , pp. 10981-10986
    • Vieillard, V.1    Strominger, J.L.2    Debré, P.3
  • 43
    • 84964864966 scopus 로고    scopus 로고
    • Broadly-reactive neutralizing and non-neutralizing antibodies directed against the H7 influenza virus hemagglutinin reveal divergent mechanisms of protection
    • Tan GS, et al. (2016) Broadly-reactive neutralizing and non-neutralizing antibodies directed against the H7 influenza virus hemagglutinin reveal divergent mechanisms of protection. PLoS Pathog 12(4):e1005578.
    • (2016) PLoS Pathog , vol.12 , Issue.4
    • Tan, G.S.1
  • 44
    • 84973488141 scopus 로고    scopus 로고
    • Both neutralizing and non-neutralizing human h7n9 influenza vaccine-induced monoclonal antibodies confer protection
    • Henry Dunand CJ, et al. (2016) Both neutralizing and non-neutralizing human h7n9 influenza vaccine-induced monoclonal antibodies confer protection. Cell Host Microbe 19(6):800-813.
    • (2016) Cell Host Microbe , vol.19 , Issue.6 , pp. 800-813
    • Henry Dunand, C.J.1
  • 45
    • 56649103827 scopus 로고    scopus 로고
    • Multiple receptors involved in human rhinovirus attachment to live cells
    • Rankl C, et al. (2008) Multiple receptors involved in human rhinovirus attachment to live cells. Proc Natl Acad Sci USA 105(46):17778-17783.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.46 , pp. 17778-17783
    • Rankl, C.1
  • 46
    • 0037770209 scopus 로고    scopus 로고
    • A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid
    • Neumann E, Moser R, Snyers L, Blaas D, Hewat EA (2003) A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid. J Virol 77(15):8504-8511.
    • (2003) J Virol , vol.77 , Issue.15 , pp. 8504-8511
    • Neumann, E.1    Moser, R.2    Snyers, L.3    Blaas, D.4    Hewat, E.A.5
  • 47
    • 0033889709 scopus 로고    scopus 로고
    • Low density lipoprotein receptor of macrophages facilitates atherosclerotic lesion formation in C57Bl/6 mice
    • Herijgers N, Van Eck M, Groot PH, Hoogerbrugge PM, Van Berkel TJ (2000) Low density lipoprotein receptor of macrophages facilitates atherosclerotic lesion formation in C57Bl/6 mice. Arterioscler Thromb Vasc Biol 20(8):1961-1967.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , Issue.8 , pp. 1961-1967
    • Herijgers, N.1    Van Eck, M.2    Groot, P.H.3    Hoogerbrugge, P.M.4    Van Berkel, T.J.5
  • 48
    • 84953298218 scopus 로고    scopus 로고
    • Respiratory syncytial virus uses CX3CR1 as a receptor on primary human airway epithelial cultures
    • Johnson SM, et al. (2015) Respiratory syncytial virus uses CX3CR1 as a receptor on primary human airway epithelial cultures. PLoS Pathog 11(12):e1005318.
    • (2015) PLoS Pathog , vol.11 , Issue.12
    • Johnson, S.M.1
  • 49
    • 84055200171 scopus 로고    scopus 로고
    • CX3CR1 regulates intestinal macrophage homeostasis, bacterial translocation, and colitogenic Th17 responses in mice
    • Medina-Contreras O, et al. (2011) CX3CR1 regulates intestinal macrophage homeostasis, bacterial translocation, and colitogenic Th17 responses in mice. J Clin Invest 121(12):4787-4795.
    • (2011) J Clin Invest , vol.121 , Issue.12 , pp. 4787-4795
    • Medina-Contreras, O.1
  • 50
    • 34147219730 scopus 로고    scopus 로고
    • Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry
    • Evans MJ, et al. (2007) Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature 446(7137):801-805.
    • (2007) Nature , vol.446 , Issue.7137 , pp. 801-805
    • Evans, M.J.1
  • 51
    • 84878378276 scopus 로고    scopus 로고
    • Characterization of tetraspanins CD9, CD53, CD63, and CD81 in monocytes and macrophages in HIV-1 infection
    • Tippett E, Cameron PU, Marsh M, Crowe SM (2013) Characterization of tetraspanins CD9, CD53, CD63, and CD81 in monocytes and macrophages in HIV-1 infection. J Leukoc Biol 93(6):913-920.
    • (2013) J Leukoc Biol , vol.93 , Issue.6 , pp. 913-920
    • Tippett, E.1    Cameron, P.U.2    Marsh, M.3    Crowe, S.M.4
  • 52
    • 77957784634 scopus 로고    scopus 로고
    • Clinical protection from falciparum malaria correlates with neutrophil respiratory bursts induced by merozoites opsonized with human serum antibodies
    • Joos C, et al. (2010) Clinical protection from falciparum malaria correlates with neutrophil respiratory bursts induced by merozoites opsonized with human serum antibodies. PLoS One 5(3):e9871.
    • (2010) PLoS One , vol.5 , Issue.3
    • Joos, C.1
  • 53
    • 67649713030 scopus 로고    scopus 로고
    • The E-selectin ligand basigin/CD147 is responsible for neutrophil recruitment in renal ischemia/reperfusion
    • Kato N, et al. (2009) The E-selectin ligand basigin/CD147 is responsible for neutrophil recruitment in renal ischemia/reperfusion. J Am Soc Nephrol 20(7):1565-1576.
    • (2009) J Am Soc Nephrol , vol.20 , Issue.7 , pp. 1565-1576
    • Kato, N.1
  • 54
    • 0023612465 scopus 로고
    • Characterization of variable-region genes and shared cross-reactive idiotypes of antibodies specific for antigens of various influenza viruses
    • Moran TM, et al. (1987) Characterization of variable-region genes and shared cross-reactive idiotypes of antibodies specific for antigens of various influenza viruses. Viral Immunol 1(1):1-12.
    • (1987) Viral Immunol , vol.1 , Issue.1 , pp. 1-12
    • Moran, T.M.1
  • 55
    • 80055108707 scopus 로고    scopus 로고
    • Generation of recombinant influenza virus from plasmid DNA
    • Martínez-Sobrido L, García-Sastre A (2010) Generation of recombinant influenza virus from plasmid DNA. J Vis Exp (42):2057.
    • (2010) J Vis Exp , Issue.42 , pp. 2057
    • Martínez-Sobrido, L.1    García-Sastre, A.2
  • 56
    • 84914152611 scopus 로고    scopus 로고
    • Development of a robust reporter-based ADCC assay with frozen, thaw-and-use cells to measure Fc effector function of therapeutic antibodies
    • Cheng ZJ, et al. (2014) Development of a robust reporter-based ADCC assay with frozen, thaw-and-use cells to measure Fc effector function of therapeutic antibodies. J Immunol Methods 414(C):69-81.
    • (2014) J Immunol Methods , vol.414 , Issue.C , pp. 69-81
    • Cheng, Z.J.1
  • 57
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera: A visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.