메뉴 건너뛰기




Volumn 428, Issue 14, 2016, Pages 2860-2879

Functional Antagonism of Human CD40 Achieved by Targeting a Unique Species-Specific Epitope

Author keywords

autoimmune disease; CD40; domain antibody; therapeutic; X ray structure

Indexed keywords

CD40 ANTIGEN; CD40 LIGAND; CD40 LIGAND MONOCLONAL ANTIBODY; EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT;

EID: 84977275336     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2016.05.014     Document Type: Article
Times cited : (15)

References (63)
  • 1
    • 2542476167 scopus 로고    scopus 로고
    • CD40/CD154 interactions at the interface of tolerance and immunity
    • [1] Quezada, S.A., Jarvinen, L.Z., Lind, E.F., Noelle, R.J., CD40/CD154 interactions at the interface of tolerance and immunity. Annu. Rev. Immunol. 22 (2004), 307–328.
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 307-328
    • Quezada, S.A.1    Jarvinen, L.Z.2    Lind, E.F.3    Noelle, R.J.4
  • 3
    • 0027293241 scopus 로고
    • The regulation of the expression of gp39, the CD40 ligand, on normal and cloned CD4 + T cells
    • [3] Roy, M., Waldschmidt, T., Aruffo, A., Ledbetter, J.A., Noelle, R.J., The regulation of the expression of gp39, the CD40 ligand, on normal and cloned CD4 + T cells. J. Immunol. 151 (1993), 2497–2510.
    • (1993) J. Immunol. , vol.151 , pp. 2497-2510
    • Roy, M.1    Waldschmidt, T.2    Aruffo, A.3    Ledbetter, J.A.4    Noelle, R.J.5
  • 4
    • 0027394391 scopus 로고
    • The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome
    • [4] Aruffo, A., Farrington, M., Hollenbaugh, D., Li, X., Milatovich, A., Nonoyama, S., et al. The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome. Cell 72 (1993), 291–300.
    • (1993) Cell , vol.72 , pp. 291-300
    • Aruffo, A.1    Farrington, M.2    Hollenbaugh, D.3    Li, X.4    Milatovich, A.5    Nonoyama, S.6
  • 6
    • 0027533185 scopus 로고
    • Defective expression of T-cell CD40 ligand causes X-linked immunodeficiency with hyper-IgM
    • [6] Korthauer, U., Graf, D., Mages, H.W., Briere, F., Padayachee, M., Malcolm, S., et al. Defective expression of T-cell CD40 ligand causes X-linked immunodeficiency with hyper-IgM. Nature 361 (1993), 539–541.
    • (1993) Nature , vol.361 , pp. 539-541
    • Korthauer, U.1    Graf, D.2    Mages, H.W.3    Briere, F.4    Padayachee, M.5    Malcolm, S.6
  • 7
    • 0027930446 scopus 로고
    • Hypogammaglobulinaemia associated with normal or increased IgM (the hyper IgM syndrome): a case series review
    • [7] Banatvala, N., Davies, J., Kanariou, M., Strobel, S., Levinsky, R., Morgan, G., Hypogammaglobulinaemia associated with normal or increased IgM (the hyper IgM syndrome): a case series review. Arch. Dis. Child. 71 (1994), 150–152.
    • (1994) Arch. Dis. Child. , vol.71 , pp. 150-152
    • Banatvala, N.1    Davies, J.2    Kanariou, M.3    Strobel, S.4    Levinsky, R.5    Morgan, G.6
  • 9
    • 0028123024 scopus 로고
    • Antibody to the ligand of CD40, gp39, blocks the occurrence of the acute and chronic forms of graft-vs-host disease
    • [9] Durie, F.H., Aruffo, A., Ledbetter, J., Crassi, K.M., Green, W.R., Fast, L.D., et al. Antibody to the ligand of CD40, gp39, blocks the occurrence of the acute and chronic forms of graft-vs-host disease. J. Clin. Invest. 94 (1994), 1333–1338.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1333-1338
    • Durie, F.H.1    Aruffo, A.2    Ledbetter, J.3    Crassi, K.M.4    Green, W.R.5    Fast, L.D.6
  • 10
    • 0027816953 scopus 로고
    • Prevention of collagen-induced arthritis with an antibody to gp39, the ligand for CD40
    • [10] Durie, F.H., Fava, R.A., Foy, T.M., Aruffo, A., Ledbetter, J.A., Noelle, R.J., Prevention of collagen-induced arthritis with an antibody to gp39, the ligand for CD40. Science 261 (1993), 1328–1330.
    • (1993) Science , vol.261 , pp. 1328-1330
    • Durie, F.H.1    Fava, R.A.2    Foy, T.M.3    Aruffo, A.4    Ledbetter, J.A.5    Noelle, R.J.6
  • 11
    • 0027930707 scopus 로고
    • The role of CD40 in the regulation of humoral and cell-mediated immunity
    • [11] Durie, F.H., Foy, T.M., Masters, S.R., Laman, J.D., Noelle, R.J., The role of CD40 in the regulation of humoral and cell-mediated immunity. Immunol. Today 15 (1994), 406–411.
    • (1994) Immunol. Today , vol.15 , pp. 406-411
    • Durie, F.H.1    Foy, T.M.2    Masters, S.R.3    Laman, J.D.4    Noelle, R.J.5
  • 14
    • 0027493906 scopus 로고
    • In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. II. Prolonged suppression of the humoral immune response by an antibody to the ligand for CD40, gp39
    • [14] Foy, T.M., Shepherd, D.M., Durie, F.H., Aruffo, A., Ledbetter, J.A., Noelle, R.J., In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. II. Prolonged suppression of the humoral immune response by an antibody to the ligand for CD40, gp39. J. Exp. Med. 178 (1993), 1567–1575.
    • (1993) J. Exp. Med. , vol.178 , pp. 1567-1575
    • Foy, T.M.1    Shepherd, D.M.2    Durie, F.H.3    Aruffo, A.4    Ledbetter, J.A.5    Noelle, R.J.6
  • 16
    • 0027373275 scopus 로고
    • In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. I. In vivo expression of CD40 ligand, cytokines, and antibody production delineates sites of cognate T–B cell interactions
    • [16] Van den Eertwegh, A.J., Noelle, R.J., Roy, M., Shepherd, D.M., Aruffo, A., Ledbetter, J.A., et al. In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. I. In vivo expression of CD40 ligand, cytokines, and antibody production delineates sites of cognate T–B cell interactions. J. Exp. Med. 178 (1993), 1555–1565.
    • (1993) J. Exp. Med. , vol.178 , pp. 1555-1565
    • Van den Eertwegh, A.J.1    Noelle, R.J.2    Roy, M.3    Shepherd, D.M.4    Aruffo, A.5    Ledbetter, J.A.6
  • 17
    • 79953154967 scopus 로고    scopus 로고
    • CD40 agonists alter tumor stroma and show efficacy against pancreatic carcinoma in mice and humans
    • [17] Beatty, G.L., Chiorean, E.G., Fishman, M.P., Saboury, B., Teitelbaum, U.R., Sun, W., et al. CD40 agonists alter tumor stroma and show efficacy against pancreatic carcinoma in mice and humans. Science 331 (2011), 1612–1616.
    • (2011) Science , vol.331 , pp. 1612-1616
    • Beatty, G.L.1    Chiorean, E.G.2    Fishman, M.P.3    Saboury, B.4    Teitelbaum, U.R.5    Sun, W.6
  • 18
    • 22844449094 scopus 로고    scopus 로고
    • Safety and tolerability of antagonist anti-human CD40 Mab ch5D12 in patients with moderate to severe Crohn's disease
    • [18] Kasran, A., Boon, L., Wortel, C.H., Hogezand, R.A., Schreiber, S., Goldin, E., et al. Safety and tolerability of antagonist anti-human CD40 Mab ch5D12 in patients with moderate to severe Crohn's disease. Aliment. Pharmacol. Ther. 22 (2005), 111–122.
    • (2005) Aliment. Pharmacol. Ther. , vol.22 , pp. 111-122
    • Kasran, A.1    Boon, L.2    Wortel, C.H.3    Hogezand, R.A.4    Schreiber, S.5    Goldin, E.6
  • 19
    • 34548580969 scopus 로고    scopus 로고
    • Anti-CD40 agonist antibodies: preclinical and clinical experience
    • [19] Khalil, M., Vonderheide, R.H., Anti-CD40 agonist antibodies: preclinical and clinical experience. Update Cancer Ther. 2 (2007), 61–65.
    • (2007) Update Cancer Ther. , vol.2 , pp. 61-65
    • Khalil, M.1    Vonderheide, R.H.2
  • 20
    • 33947223664 scopus 로고    scopus 로고
    • Prospect of targeting the CD40 pathway for cancer therapy
    • [20] Vonderheide, R.H., Prospect of targeting the CD40 pathway for cancer therapy. Clin. Cancer Res. 13 (2007), 1083–1088.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1083-1088
    • Vonderheide, R.H.1
  • 22
    • 84934443973 scopus 로고    scopus 로고
    • Creation of the large and highly functional synthetic repertoire of human VH and Vkappa domain antibodies
    • [22] Ignatovich, O., Jespers, L., Tomlinson, I.M., de Wildt, R.M., Creation of the large and highly functional synthetic repertoire of human VH and Vkappa domain antibodies. Methods Mol. Biol. 911 (2012), 39–63.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 39-63
    • Ignatovich, O.1    Jespers, L.2    Tomlinson, I.M.3    de Wildt, R.M.4
  • 23
    • 0025226085 scopus 로고
    • Phage antibodies: filamentous phage displaying antibody variable domains
    • [23] McCafferty, J., Griffiths, A.D., Winter, G., Chiswell, D.J., Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348 (1990), 552–554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 24
    • 0035881236 scopus 로고    scopus 로고
    • Biophysical characterization of a soluble CD40 ligand (CD154) coiled-coil trimer: evidence of a reversible acid-denatured molten globule
    • [24] Matsuura, J.E., Morris, A.E., Ketchem, R.R., Braswell, E.H., Klinke, R., Gombotz, W.R., et al. Biophysical characterization of a soluble CD40 ligand (CD154) coiled-coil trimer: evidence of a reversible acid-denatured molten globule. Arch. Biochem. Biophys. 392 (2001), 208–218.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 208-218
    • Matsuura, J.E.1    Morris, A.E.2    Ketchem, R.R.3    Braswell, E.H.4    Klinke, R.5    Gombotz, W.R.6
  • 25
    • 0010982635 scopus 로고
    • Activation of human B cells mediated through two distinct cell surface differentiation antigens, Bp35 and Bp50
    • [25] Clark, E.A., Ledbetter, J.A., Activation of human B cells mediated through two distinct cell surface differentiation antigens, Bp35 and Bp50. Proc. Natl. Acad. Sci. U. S. A. 83 (1986), 4494–4498.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4494-4498
    • Clark, E.A.1    Ledbetter, J.A.2
  • 26
    • 19944412462 scopus 로고    scopus 로고
    • Development of a chimeric anti-CD40 monoclonal antibody that synergizes with LEA29Y to prolong islet allograft survival
    • [26] Adams, A.B., Shirasugi, N., Jones, T.R., Durham, M.M., Strobert, E.A., Cowan, S., et al. Development of a chimeric anti-CD40 monoclonal antibody that synergizes with LEA29Y to prolong islet allograft survival. J. Immunol. 174 (2005), 542–550.
    • (2005) J. Immunol. , vol.174 , pp. 542-550
    • Adams, A.B.1    Shirasugi, N.2    Jones, T.R.3    Durham, M.M.4    Strobert, E.A.5    Cowan, S.6
  • 27
    • 79959549552 scopus 로고    scopus 로고
    • Beamline 08ID-1, the prime beamline of the Canadian macromolecular crystallography facility
    • [27] Grochulski, P., Fodje, M.N., Gorin, J., Labiuk, S.L., Berg, R., Beamline 08ID-1, the prime beamline of the Canadian macromolecular crystallography facility. J. Synchrotron Radiat. 18 (2011), 681–684.
    • (2011) J. Synchrotron Radiat. , vol.18 , pp. 681-684
    • Grochulski, P.1    Fodje, M.N.2    Gorin, J.3    Labiuk, S.L.4    Berg, R.5
  • 28
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • [28] Kabsch, W., Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. Sect. D: Biol. Crystallogr. 66 (2010), 133–144.
    • (2010) Acta Crystallogr. Sect. D: Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 29
    • 76449099287 scopus 로고    scopus 로고
    • XDS, Acta Crystallographica section D
    • [29] Kabsch, W., XDS, Acta Crystallographica section D. Biol. Crystallogr. 66 (2010), 125–132.
    • (2010) Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Carter Sweet
    • [30] Otwinowski, Z.W., Minor, W., Processing of X-ray Diffraction Data Collected in Oscillation Mode. Carter, Sweet, (eds.) Methods Enzymol, Macromolecular Crystallography Part A, 276, 1997, 307–326.
    • (1997) Methods Enzymol, Macromolecular Crystallography Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.W.1    Minor, W.2
  • 33
    • 0000541786 scopus 로고
    • Some methods for examining the interactions between two molecules
    • [33] Sheriff, S., Some methods for examining the interactions between two molecules. ImmunoMethods 3 (1993), 191–196.
    • (1993) ImmunoMethods , vol.3 , pp. 191-196
    • Sheriff, S.1
  • 34
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution
    • [34] Sheriff, S., Hendrickson, W.A., Smith, J.L., Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution. J. Mol. Biol. 197 (1987), 273–296.
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 35
    • 0002583957 scopus 로고
    • Joint CCP4 and ESF-EACBM newsletter on protein crystallography
    • [35] Cowtan, K., Joint CCP4 and ESF-EACBM newsletter on protein crystallography., 31, 1994, 34–38.
    • (1994) , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 36
    • 33744820336 scopus 로고
    • Number 4
    • [36] Collaborative Computational Project. Number 4. Acta Crystallogr. D Biol. Crystallogr. 50 (1994), 760–763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 37
    • 0035451355 scopus 로고    scopus 로고
    • Prevention of experimental autoimmune encephalomyelitis in the common marmoset (Callithrix jacchus) using a chimeric antagonist monoclonal antibody against human CD40 is associated with altered B cell responses
    • [37] Boon, L., Brok, H.P., Bauer, J., Ortiz-Buijsse, A., Schellekens, M.M., Ramdien-Murli, S., et al. Prevention of experimental autoimmune encephalomyelitis in the common marmoset (Callithrix jacchus) using a chimeric antagonist monoclonal antibody against human CD40 is associated with altered B cell responses. J. Immunol. 167 (2001), 2942–2949.
    • (2001) J. Immunol. , vol.167 , pp. 2942-2949
    • Boon, L.1    Brok, H.P.2    Bauer, J.3    Ortiz-Buijsse, A.4    Schellekens, M.M.5    Ramdien-Murli, S.6
  • 39
    • 37349029002 scopus 로고    scopus 로고
    • A novel fully human anti-CD40 monoclonal antibody, 4D11, for kidney transplantation in cynomolgus monkeys
    • [39] Imai, A., Suzuki, T., Sugitani, A., Itoh, T., Ueki, S., Aoyagi, T., et al. A novel fully human anti-CD40 monoclonal antibody, 4D11, for kidney transplantation in cynomolgus monkeys. Transplantation 84 (2007), 1020–1028.
    • (2007) Transplantation , vol.84 , pp. 1020-1028
    • Imai, A.1    Suzuki, T.2    Sugitani, A.3    Itoh, T.4    Ueki, S.5    Aoyagi, T.6
  • 40
    • 0029946329 scopus 로고    scopus 로고
    • Functions of CD40 and its ligand, gp39 (CD40L)
    • [40] Laman, J.D., Claassen, E., Noelle, R.J., Functions of CD40 and its ligand, gp39 (CD40L). Crit. Rev. Immunol. 16 (1996), 59–108.
    • (1996) Crit. Rev. Immunol. , vol.16 , pp. 59-108
    • Laman, J.D.1    Claassen, E.2    Noelle, R.J.3
  • 41
    • 0036687834 scopus 로고    scopus 로고
    • Protection of marmoset monkeys against EAE by treatment with a murine antibody blocking CD40 (mu5D12)
    • [41] Laman, J.D., BA, t.'t.H.H., Brok, H., Meurs, M., MM, S., Kasran, A., et al. Protection of marmoset monkeys against EAE by treatment with a murine antibody blocking CD40 (mu5D12). Eur. J. Immunol. 32 (2002), 2218–2228.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2218-2228
    • Laman, J.D.1    BA, T.'T.H.H.2    Brok, H.3    Meurs, M.4    MM, S.5    Kasran, A.6
  • 42
    • 84863190818 scopus 로고    scopus 로고
    • Long-term hepatic allograft acceptance based on CD40 blockade by ASKP1240 in nonhuman primates
    • [42] Oura, T., Yamashita, K., Suzuki, T., Fukumori, D., Watanabe, M., Hirokata, G., et al. Long-term hepatic allograft acceptance based on CD40 blockade by ASKP1240 in nonhuman primates. Am. J. Transplant. 12 (2012), 1740–1754.
    • (2012) Am. J. Transplant. , vol.12 , pp. 1740-1754
    • Oura, T.1    Yamashita, K.2    Suzuki, T.3    Fukumori, D.4    Watanabe, M.5    Hirokata, G.6
  • 43
    • 0028899395 scopus 로고
    • Identification of residues on CD40 and its ligand which are critical for the receptor-ligand interaction
    • [43] Bajorath, J., Chalupny, N.J., Marken, J.S., Siadak, A.W., Skonier, J., Gordon, M., et al. Identification of residues on CD40 and its ligand which are critical for the receptor-ligand interaction. Biochemistry 34 (1995), 1833–1844.
    • (1995) Biochemistry , vol.34 , pp. 1833-1844
    • Bajorath, J.1    Chalupny, N.J.2    Marken, J.S.3    Siadak, A.W.4    Skonier, J.5    Gordon, M.6
  • 44
    • 0029128893 scopus 로고
    • Analysis of gp39/CD40 interactions using molecular models and site-directed mutagenesis
    • [44] Bajorath, J., Marken, J.S., Chalupny, N.J., Spoon, T.L., Siadak, A.W., Gordon, M., et al. Analysis of gp39/CD40 interactions using molecular models and site-directed mutagenesis. Biochemistry 34 (1995), 9884–9892.
    • (1995) Biochemistry , vol.34 , pp. 9884-9892
    • Bajorath, J.1    Marken, J.S.2    Chalupny, N.J.3    Spoon, T.L.4    Siadak, A.W.5    Gordon, M.6
  • 45
    • 79953229244 scopus 로고    scopus 로고
    • Crystallographic and mutational analysis of the CD40-CD154 complex and its implications for receptor activation
    • [45] An, H.J., Kim, Y.J., Song, D.H., Park, B.S., Kim, H.M., Lee, J.D., et al. Crystallographic and mutational analysis of the CD40-CD154 complex and its implications for receptor activation. J. Biol. Chem. 286 (2011), 11,226–11,235.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11226-11235
    • An, H.J.1    Kim, Y.J.2    Song, D.H.3    Park, B.S.4    Kim, H.M.5    Lee, J.D.6
  • 47
    • 0026705933 scopus 로고
    • Identification of cysteine-rich domains of the type 1 tumor necrosis factor receptor involved in ligand binding
    • [47] Marsters, S.A., Frutkin, A.D., Simpson, N.J., Fendly, B.M., Ashkenazi, A., Identification of cysteine-rich domains of the type 1 tumor necrosis factor receptor involved in ligand binding. J. Biol. Chem. 267 (1992), 5747–5750.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5747-5750
    • Marsters, S.A.1    Frutkin, A.D.2    Simpson, N.J.3    Fendly, B.M.4    Ashkenazi, A.5
  • 48
    • 0031836472 scopus 로고    scopus 로고
    • The role of polar interactions in the molecular recognition of CD40L with its receptor CD40
    • [48] Singh, J., Garber, E., Van Vlijmen, H., Karpusas, M., Hsu, Y.M., Zheng, Z., et al. The role of polar interactions in the molecular recognition of CD40L with its receptor CD40. Protein Sci. Publ. Prot. Soc. 7 (1998), 1124–1135.
    • (1998) Protein Sci. Publ. Prot. Soc. , vol.7 , pp. 1124-1135
    • Singh, J.1    Garber, E.2    Van Vlijmen, H.3    Karpusas, M.4    Hsu, Y.M.5    Zheng, Z.6
  • 49
    • 0028566985 scopus 로고
    • Agonistic and antagonistic properties of CD40 mAb G28-5 are dependent on binding valency
    • [49] Ledbetter, J.A., Grosmaire, L.S., Hollenbaugh, D., Aruffo, A., Nadler, S.G., Agonistic and antagonistic properties of CD40 mAb G28-5 are dependent on binding valency. Circ. Shock. 44 (1994), 67–72.
    • (1994) Circ. Shock. , vol.44 , pp. 67-72
    • Ledbetter, J.A.1    Grosmaire, L.S.2    Hollenbaugh, D.3    Aruffo, A.4    Nadler, S.G.5
  • 51
    • 0035129957 scopus 로고    scopus 로고
    • Functional activity of CD40 antibodies correlates to the position of binding relative to CD154
    • [51] Barr, T.A., Heath, A.W., Functional activity of CD40 antibodies correlates to the position of binding relative to CD154. Immunology 102 (2001), 39–43.
    • (2001) Immunology , vol.102 , pp. 39-43
    • Barr, T.A.1    Heath, A.W.2
  • 52
    • 79959746703 scopus 로고    scopus 로고
    • The CD40 agonist antibody CP-870,893 enhances dendritic cell and B cell activity and promotes anti-tumor efficacy in SCID-hu mice
    • [52] Gladue, R.P., Paradis, T., Cole, S.H., Donovan, C., Nelson, R., Alpert, R., et al. The CD40 agonist antibody CP-870,893 enhances dendritic cell and B cell activity and promotes anti-tumor efficacy in SCID-hu mice. Cancer Immunol. Immunother.: CII 60 (2011), 1009–1017.
    • (2011) Cancer Immunol. Immunother.: CII , vol.60 , pp. 1009-1017
    • Gladue, R.P.1    Paradis, T.2    Cole, S.H.3    Donovan, C.4    Nelson, R.5    Alpert, R.6
  • 53
    • 0033005572 scopus 로고    scopus 로고
    • Epitope-dependent synergism and antagonism between CD40 antibodies and soluble CD40 ligand for the regulation of CD23 expression and IgE synthesis in human B cells
    • [53] Challa, A., Pound, J.D., Armitage, R.J., Gordon, J., Epitope-dependent synergism and antagonism between CD40 antibodies and soluble CD40 ligand for the regulation of CD23 expression and IgE synthesis in human B cells. Allergy 54 (1999), 576–583.
    • (1999) Allergy , vol.54 , pp. 576-583
    • Challa, A.1    Pound, J.D.2    Armitage, R.J.3    Gordon, J.4
  • 54
    • 0032926595 scopus 로고    scopus 로고
    • Minimal cross-linking and epitope requirements for CD40-dependent suppression of apoptosis contrast with those for promotion of the cell cycle and homotypic adhesions in human B cells
    • [54] Pound, J.D., Challa, A., Holder, M.J., Armitage, R.J., Dower, S.K., Fanslow, W.C., et al. Minimal cross-linking and epitope requirements for CD40-dependent suppression of apoptosis contrast with those for promotion of the cell cycle and homotypic adhesions in human B cells. Int. Immunol. 11 (1999), 11–20.
    • (1999) Int. Immunol. , vol.11 , pp. 11-20
    • Pound, J.D.1    Challa, A.2    Holder, M.J.3    Armitage, R.J.4    Dower, S.K.5    Fanslow, W.C.6
  • 55
    • 0028041170 scopus 로고
    • Monoclonal antibodies to murine CD40 define two distinct functional epitopes
    • [55] Heath, A.W., Wu, W.W., Howard, M.C., Monoclonal antibodies to murine CD40 define two distinct functional epitopes. Eur. J. Immunol. 24 (1994), 1828–1834.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1828-1834
    • Heath, A.W.1    Wu, W.W.2    Howard, M.C.3
  • 56
    • 80051925907 scopus 로고    scopus 로고
    • Interaction with FcgammaRIIB is critical for the agonistic activity of anti-CD40 monoclonal antibody
    • [56] White, A.L., Chan, H.T., Roghanian, A., French, R.R., Mockridge, C.I., Tutt, A.L., et al. Interaction with FcgammaRIIB is critical for the agonistic activity of anti-CD40 monoclonal antibody. J. Immunol. 187 (2011), 1754–1763.
    • (2011) J. Immunol. , vol.187 , pp. 1754-1763
    • White, A.L.1    Chan, H.T.2    Roghanian, A.3    French, R.R.4    Mockridge, C.I.5    Tutt, A.L.6
  • 57
    • 80051885494 scopus 로고    scopus 로고
    • Inhibitory Fcgamma receptor engagement drives adjuvant and anti-tumor activities of agonistic CD40 antibodies
    • [57] Li, F., Ravetch, J.V., Inhibitory Fcgamma receptor engagement drives adjuvant and anti-tumor activities of agonistic CD40 antibodies. Science 333 (2011), 1030–1034.
    • (2011) Science , vol.333 , pp. 1030-1034
    • Li, F.1    Ravetch, J.V.2
  • 58
    • 84938603871 scopus 로고    scopus 로고
    • Anti-human CD40 monoclonal antibody therapy is potent without FcR crosslinking
    • e28610
    • [58] Richman, L.P., Vonderheide, R.H., Anti-human CD40 monoclonal antibody therapy is potent without FcR crosslinking. Oncoimmunology, 3, 2014, e28610.
    • (2014) Oncoimmunology , vol.3
    • Richman, L.P.1    Vonderheide, R.H.2
  • 59
    • 84922189761 scopus 로고    scopus 로고
    • Conformation of the human immunoglobulin g2 hinge imparts superagonistic properties to immunostimulatory anticancer antibodies
    • [59] White, A.L., Chan, H.T., French, R.R., Willoughby, J., Mockridge, C.I., Roghanian, A., et al. Conformation of the human immunoglobulin g2 hinge imparts superagonistic properties to immunostimulatory anticancer antibodies. Cancer Cell 27 (2015), 138–148.
    • (2015) Cancer Cell , vol.27 , pp. 138-148
    • White, A.L.1    Chan, H.T.2    French, R.R.3    Willoughby, J.4    Mockridge, C.I.5    Roghanian, A.6
  • 60
    • 0036039462 scopus 로고    scopus 로고
    • Modulation of the CD40–CD40 ligand interaction using human anti-CD40 single-chain antibody fragments obtained from the n-CoDeR phage display library
    • [60] Ellmark, P., Ottosson, C., Borrebaeck, C.A., Malmborg Hager, A.C., Furebring, C., Modulation of the CD40–CD40 ligand interaction using human anti-CD40 single-chain antibody fragments obtained from the n-CoDeR phage display library. Immunology 106 (2002), 456–463.
    • (2002) Immunology , vol.106 , pp. 456-463
    • Ellmark, P.1    Ottosson, C.2    Borrebaeck, C.A.3    Malmborg Hager, A.C.4    Furebring, C.5
  • 61
    • 84878225457 scopus 로고    scopus 로고
    • Design of synthetic autonomous VH domain libraries and structural analysis of a VH domain bound to vascular endothelial growth factor
    • [61] Ma, X., Barthelemy, P.A., Rouge, L., Wiesmann, C., Sidhu, S.S., Design of synthetic autonomous VH domain libraries and structural analysis of a VH domain bound to vascular endothelial growth factor. J. Mol. Biol. 425 (2013), 2247–2259.
    • (2013) J. Mol. Biol. , vol.425 , pp. 2247-2259
    • Ma, X.1    Barthelemy, P.A.2    Rouge, L.3    Wiesmann, C.4    Sidhu, S.S.5
  • 62
    • 84856764818 scopus 로고    scopus 로고
    • Structures of adnectin/protein complexes reveal an expanded binding footprint
    • [62] Ramamurthy, V., Krystek, S.R. Jr., Bush, A., Wei, A., Emanuel, S.L., Das Gupta, R., et al. Structures of adnectin/protein complexes reveal an expanded binding footprint. Structure 20 (2012), 259–269.
    • (2012) Structure , vol.20 , pp. 259-269
    • Ramamurthy, V.1    Krystek, S.R.2    Bush, A.3    Wei, A.4    Emanuel, S.L.5    Das Gupta, R.6
  • 63
    • 79961092776 scopus 로고    scopus 로고
    • Small molecule inhibition of the TNF family cytokine CD40 ligand through a subunit fracture mechanism
    • [63] Silvian, L.F., Friedman, J.E., Strauch, K., Cachero, T.G., Day, E.S., Qian, F., et al. Small molecule inhibition of the TNF family cytokine CD40 ligand through a subunit fracture mechanism. ACS Chem. Biol. 6 (2011), 636–647.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 636-647
    • Silvian, L.F.1    Friedman, J.E.2    Strauch, K.3    Cachero, T.G.4    Day, E.S.5    Qian, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.