메뉴 건너뛰기




Volumn 491, Issue 7425, 2012, Pages 613-617

Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

E2 79; FC RECEPTOR; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E FC EPSILON RECEPTOR IALPHA COMPLEX; OMALIZUMAB; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 84869880199     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11546     Document Type: Article
Times cited : (91)

References (34)
  • 1
    • 34247572895 scopus 로고    scopus 로고
    • New developments in FceRI regulation, function and inhibition
    • Kraft, S. & Kinet, J. P. New developments in FceRI regulation, function and inhibition. Nature Rev. Immunol. 7, 365-378 (2007).
    • (2007) Nature Rev. Immunol. , vol.7 , pp. 365-378
    • Kraft, S.1    Kinet, J.P.2
  • 2
    • 40049101678 scopus 로고    scopus 로고
    • IgE in allergy and asthma today
    • Gould, H. J. & Sutton, B. J. IgE in allergy and asthma today. Nature Rev. Immunol. 8, 205-217 (2008).
    • (2008) Nature Rev. Immunol. , vol.8 , pp. 205-217
    • Gould, H.J.1    Sutton, B.J.2
  • 3
    • 33845699468 scopus 로고    scopus 로고
    • Treating moderate-to-severe allergic asthma with a recombinant humanized anti-IgE monoclonal antibody (Omalizumab)
    • D'Amato, G., Bucchioni, E., Oldani, V. & Canonica, W. Treating moderate-to-severe allergic asthma with a recombinant humanized anti-IgE monoclonal antibody (Omalizumab). Treat. Respir. Med. 5, 393-398 (2006).
    • (2006) Treat. Respir. Med. , vol.5 , pp. 393-398
    • D'Amato, G.1    Bucchioni, E.2    Oldani, V.3    Canonica, W.4
  • 4
    • 0000898623 scopus 로고    scopus 로고
    • The pharmacological basis of anti-IgE therapy
    • Chang, T. W. The pharmacological basis of anti-IgE therapy. Nature Biotechnol. 18, 157-162 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 157-162
    • Chang, T.W.1
  • 5
    • 79955603056 scopus 로고    scopus 로고
    • Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FceRI
    • Holdom, M. D. et al. Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FceRI. Nature Struct. Mol. Biol. 18, 571-576 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 571-576
    • Holdom, M.D.1
  • 6
    • 84864497135 scopus 로고    scopus 로고
    • Crystal structureofIgE boundtoits B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor FceRI
    • Dhaliwal, B. et al. Crystal structureofIgE boundtoits B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor FceRI. Proc. Natl Acad. Sci. USA 109, 12686-12691 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 12686-12691
    • Dhaliwal, B.1
  • 8
    • 0033673325 scopus 로고    scopus 로고
    • StructureofthehumanIgE-FcCe3-Ce4 reveals conformational flexibility in the antibody effector domains
    • Wurzburg, B. A., Garman, S. C. & Jardetzky, T. S. StructureofthehumanIgE-FcCe3-Ce4 reveals conformational flexibility in the antibody effector domains. Immunity 13, 375-385 (2000).
    • (2000) Immunity , vol.13 , pp. 375-385
    • Wurzburg, B.A.1    Garman, S.C.2    Jardetzky, T.S.3
  • 9
    • 70349784988 scopus 로고    scopus 로고
    • DARPins as bispecific receptor antagonists analyzed for immunoglobulinE receptor blockage
    • Eggel, A., Baumann, M. J., Amstutz, P., Stadler, B. M. & Vogel, M. DARPins as bispecific receptor antagonists analyzed for immunoglobulinE receptor blockage. J. Mol. Biol. 393, 598-607 (2009).
    • (2009) J. Mol. Biol. , vol.393 , pp. 598-607
    • Eggel, A.1    Baumann, M.J.2    Amstutz, P.3    Stadler, B.M.4    Vogel, M.5
  • 11
    • 79958110928 scopus 로고    scopus 로고
    • Inhibition of ongoing allergic reactions using a novel anti-IgE DARPin-Fc fusion protein
    • Eggel, A. et al. Inhibition of ongoing allergic reactions using a novel anti-IgE DARPin-Fc fusion protein. Allergy 66, 961-968 (2011).
    • (2011) Allergy , vol.66 , pp. 961-968
    • Eggel, A.1
  • 12
    • 0034691520 scopus 로고    scopus 로고
    • Structure of the Fc fragment of human IgE bound to its high-affinity receptor FceRIa
    • Garman, S. C., Wurzburg, B. A., Tarchevskaya, S. S., Kinet, J. P. & Jardetzky, T. S. Structure of the Fc fragment of human IgE bound to its high-affinity receptor FceRIa. Nature 406, 259-266 (2000).
    • (2000) Nature , vol.406 , pp. 259-266
    • Garman, S.C.1    Wurzburg, B.A.2    Tarchevskaya, S.S.3    Kinet, J.P.4    Jardetzky, T.S.5
  • 13
    • 0027444617 scopus 로고
    • Purification and characterization of human recombinant IgE-Fc fragments that bind to the human high affinity IgE receptor
    • Basu, M. et al. Purification and characterization of human recombinant IgE-Fc fragments that bind to the human high affinity IgE receptor. J. Biol. Chem. 268, 13118-13127 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 13118-13127
    • Basu, M.1
  • 14
    • 0026583666 scopus 로고
    • Epidermal Langerhans cells from normal human skin bind monomeric IgE via FceRI
    • Wang, B. et al. Epidermal Langerhans cells from normal human skin bind monomeric IgE via FceRI. J. Exp. Med. 175, 1353-1365 (1992).
    • (1992) J. Exp. Med. , vol.175 , pp. 1353-1365
    • Wang, B.1
  • 15
    • 33947420879 scopus 로고    scopus 로고
    • Inhibition of human cord blood-derived mast cell responses by anti-FceRI mAb 15/1 versus anti-IgE Omalizumab
    • Mirkina, I., Schweighoffer, T. & Kricek, F. Inhibition of human cord blood-derived mast cell responses by anti-FceRI mAb 15/1 versus anti-IgE Omalizumab. Immunol. Lett. 109, 120-128 (2007).
    • (2007) Immunol. Lett. , vol.109 , pp. 120-128
    • Mirkina, I.1    Schweighoffer, T.2    Kricek, F.3
  • 16
    • 4544303216 scopus 로고    scopus 로고
    • In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis
    • Mendonsa, S. D. & Bowser, M. T. In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis. Anal. Chem. 76, 5387-5392 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 5387-5392
    • Mendonsa, S.D.1    Bowser, M.T.2
  • 17
    • 0029943440 scopus 로고    scopus 로고
    • High-affinity oligonucleotide ligands to human IgE inhibit binding to Fce receptor i
    • Wiegand, T. W. et al. High-affinity oligonucleotide ligands to human IgE inhibit binding to Fce receptor I. J. Immunol. 157, 221-230 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 221-230
    • Wiegand, T.W.1
  • 18
    • 51449106743 scopus 로고    scopus 로고
    • Fine epitope mapping of humanized anti-IgE monoclonal antibody omalizumab
    • Zheng, L. et al. Fine epitope mapping of humanized anti-IgE monoclonal antibody omalizumab. Biochem. Biophys. Res. Commun. 375, 619-622 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.375 , pp. 619-622
    • Zheng, L.1
  • 19
    • 0031872148 scopus 로고    scopus 로고
    • Prediction of an anti-IgE binding site on IgE
    • Wright, J. D. & Lim, C. Prediction of an anti-IgE binding site on IgE. Protein Eng. 11, 421-427 (1998).
    • (1998) Protein Eng. , vol.11 , pp. 421-427
    • Wright, J.D.1    Lim, C.2
  • 20
    • 84867765150 scopus 로고    scopus 로고
    • 3-4 in a closed, non-receptor binding conformation
    • 3-4 in a closed, non-receptor binding conformation. J. Biol. Chem. http://dx.doi.org/10.1074/jbc.M112.407502jbcM112.407502 (2012).
    • (2012) J. Biol. Chem
    • Wurzburg, B.A.1
  • 21
    • 0027265394 scopus 로고
    • 21 channels is simply explained by competition for individual attachment points
    • 21 channels is simply explained by competition for individual attachment points. J. Biol. Chem. 268, 18580-18585 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18580-18585
    • Prinz, H.1    Striessnig, J.2
  • 23
    • 33845368513 scopus 로고    scopus 로고
    • COPASI\a COmplex PAthway SImulator
    • Hoops, S. et al. COPASI\a COmplex PAthway SImulator. Bioinformatics 22, 3067-3074 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 3067-3074
    • Hoops, S.1
  • 24
    • 27744586067 scopus 로고    scopus 로고
    • Small-molecule inhibition of TNF-a
    • He, M. M. et al. Small-molecule inhibition of TNF-a. Science 310, 1022-1025 (2005).
    • (2005) Science , vol.310 , pp. 1022-1025
    • He, M.M.1
  • 25
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A. & McClendon, C. L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 (2007).
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 26
    • 0024266267 scopus 로고
    • Negative and positive site-site interactions, and their modulation by pH, insulin analogs, and monoclonal antibodies, are preserved in the purified insulin receptor
    • Wang, C. C. et al. Negative and positive site-site interactions, and their modulation by pH, insulin analogs, and monoclonal antibodies, are preserved in the purified insulin receptor. Proc. Natl Acad. Sci. USA 85, 8400-8404 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8400-8404
    • Wang, C.C.1
  • 27
    • 0022178893 scopus 로고
    • High and low affinity IL 2 receptors: Analysis by IL 2 dissociation rate and reactivity with monoclonal anti-receptor antibody PC61
    • Lowenthal, J. W. et al. High and low affinity IL 2 receptors: analysis by IL 2 dissociation rate and reactivity with monoclonal anti-receptor antibody PC61. J. Immunol. 135, 3988-3994 (1985).
    • (1985) J. Immunol. , vol.135 , pp. 3988-3994
    • Lowenthal, J.W.1
  • 28
    • 0019940814 scopus 로고
    • Neurotoxin-specific immunoglobulins accelerate dissociation of the neurotoxin-acetylcholine receptor complex
    • Boulain, J. C. & Menez, A. Neurotoxin-specific immunoglobulins accelerate dissociation of the neurotoxin-acetylcholine receptor complex. Science 217, 732-733 (1982).
    • (1982) Science , vol.217 , pp. 732-733
    • Boulain, J.C.1    Menez, A.2
  • 29
    • 0032419721 scopus 로고    scopus 로고
    • Crystal structure of the human high-affinity IgE receptor
    • Garman, S. C., Kinet, J. P. & Jardetzky, T. S. Crystal structure of the human high-affinity IgE receptor. Cell 95, 951-961 (1998).
    • (1998) Cell , vol.95 , pp. 951-961
    • Garman, S.C.1    Kinet, J.P.2    Jardetzky, T.S.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds Carter, J. C. W. & Sweet, R. M. Academic
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. inMethods Enzymol. Vol. 276 (eds Carter, J. C. W. & Sweet, R. M.) 307-326 (Academic, 1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 33
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 34
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.