메뉴 건너뛰기




Volumn 136, Issue 1, 2015, Pages 29-37.e10

100 Years later: Celebrating the contributions of x-ray crystallography to allergy and clinical immunology

Author keywords

Allergens; allergy; cross reactivity; function; structure; x ray crystallography

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E; PROTEIN BINDING;

EID: 84949124325     PISSN: 00916749     EISSN: 10976825     Source Type: Journal    
DOI: 10.1016/j.jaci.2015.05.016     Document Type: Article
Times cited : (32)

References (126)
  • 2
    • 85045225778 scopus 로고
    • X-ray photographs of crystalline pepsin
    • D. Crowfoot, and J.D. Bernal X-ray photographs of crystalline pepsin Nature 133 1934 794 795
    • (1934) Nature , vol.133 , pp. 794-795
    • Crowfoot, D.1    Bernal, J.D.2
  • 4
    • 36949066642 scopus 로고
    • Structure of haemoglobin: A three-dimensional Fourier synthesis at 5.5-A. Resolution, obtained by X-ray analysis
    • M.F. Perutz, M.G. Rossmann, A.F. Cullis, H. Muirhead, G. Will, and A.C. North Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis Nature 185 1960 416 422
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.6
  • 5
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution
    • C.C. Blake, D.F. Koenig, G.A. Mair, A.C. North, D.C. Phillips, and V.R. Sarma Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution Nature 206 1965 757 761
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.4    Phillips, D.C.5    Sarma, V.R.6
  • 6
    • 77954070786 scopus 로고    scopus 로고
    • Impact of synchrotron radiation on macromolecular crystallography: A personal view
    • Z. Dauter, M. Jaskolski, and A. Wlodawer Impact of synchrotron radiation on macromolecular crystallography: a personal view J Synchrotron Radiat 17 2010 433 444
    • (2010) J Synchrotron Radiat , vol.17 , pp. 433-444
    • Dauter, Z.1    Jaskolski, M.2    Wlodawer, A.3
  • 8
    • 84896796428 scopus 로고    scopus 로고
    • Crystallography at 100. Going from strength to strength. Introduction
    • R. Coontz, J. Fahrenkamp-Uppenbrink, M. Lavine, and V. Vinson Crystallography at 100. Going from strength to strength. Introduction Science 343 2014 1091
    • (2014) Science , vol.343 , pp. 1091
    • Coontz, R.1    Fahrenkamp-Uppenbrink, J.2    Lavine, M.3    Vinson, V.4
  • 10
    • 77955503753 scopus 로고    scopus 로고
    • Der p 5 crystal structure provides insight into the group 5 dust mite allergens
    • G.A. Mueller, R.A. Gosavi, J.M. Krahn, L.L. Edwards, M.J. Cuneo, J. Glesner, and et al. Der p 5 crystal structure provides insight into the group 5 dust mite allergens J Biol Chem 285 2010 25394 25401
    • (2010) J Biol Chem , vol.285 , pp. 25394-25401
    • Mueller, G.A.1    Gosavi, R.A.2    Krahn, J.M.3    Edwards, L.L.4    Cuneo, M.J.5    Glesner, J.6
  • 11
    • 79958149376 scopus 로고    scopus 로고
    • Ara h 2: Crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity
    • G.A. Mueller, R.A. Gosavi, A. Pomés, S. Wunschmann, A.F. Moon, R.E. London, and et al. Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity Allergy 66 2011 878 885
    • (2011) Allergy , vol.66 , pp. 878-885
    • Mueller, G.A.1    Gosavi, R.A.2    Pomés, A.3    Wunschmann, S.4    Moon, A.F.5    London, R.E.6
  • 12
    • 85028094245 scopus 로고    scopus 로고
    • The novel structure of the cockroach allergen Bla g 1 has implications for allergenicity and exposure assessment
    • G.A. Mueller, L.C. Pedersen, F.B. Lih, J. Glesner, A.F. Moon, M.D. Chapman, and et al. The novel structure of the cockroach allergen Bla g 1 has implications for allergenicity and exposure assessment J Allergy Clin Immunol 132 2013 1420 1426
    • (2013) J Allergy Clin Immunol , vol.132 , pp. 1420-1426
    • Mueller, G.A.1    Pedersen, L.C.2    Lih, F.B.3    Glesner, J.4    Moon, A.F.5    Chapman, M.D.6
  • 14
    • 84928560614 scopus 로고    scopus 로고
    • Structure of the E. Coli ribosome-EF-Tu complex at <3 Å resolution by C-corrected cryo-EM
    • N. Fischer, P. Neumann, A.L. Konevega, L.V. Bock, R. Ficner, M.V. Rodnina, and et al. Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by C-corrected cryo-EM Nature 520 2015 567 570
    • (2015) Nature , vol.520 , pp. 567-570
    • Fischer, N.1    Neumann, P.2    Konevega, A.L.3    Bock, L.V.4    Ficner, R.5    Rodnina, M.V.6
  • 16
    • 0034657790 scopus 로고    scopus 로고
    • Strategies for macromolecular synchrotron crystallography
    • W. Minor, D. Tomchick, and Z. Otwinowski Strategies for macromolecular synchrotron crystallography Structure 8 2000 R105 R110
    • (2000) Structure , vol.8 , pp. R105-R110
    • Minor, W.1    Tomchick, D.2    Otwinowski, Z.3
  • 17
    • 46749097923 scopus 로고    scopus 로고
    • Determination of protein structures-a series of fortunate events
    • M. Chruszcz, A. Wlodawer, and W. Minor Determination of protein structures-a series of fortunate events Biophys J 95 2008 1 9
    • (2008) Biophys J , vol.95 , pp. 1-9
    • Chruszcz, M.1    Wlodawer, A.2    Minor, W.3
  • 18
    • 37349016530 scopus 로고    scopus 로고
    • Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures
    • A. Wlodawer, W. Minor, Z. Dauter, and M. Jaskolski Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures FEBS J 275 2008 1 21
    • (2008) FEBS J , vol.275 , pp. 1-21
    • Wlodawer, A.1    Minor, W.2    Dauter, Z.3    Jaskolski, M.4
  • 20
    • 84907810174 scopus 로고    scopus 로고
    • Avoidable errors in deposited macromolecular structures: An impediment to efficient data mining
    • Z. Dauter, A. Wlodawer, W. Minor, M. Jaskolski, and B. Rupp Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining IUCrJ 1 2014 179 193
    • (2014) IUCrJ , vol.1 , pp. 179-193
    • Dauter, Z.1    Wlodawer, A.2    Minor, W.3    Jaskolski, M.4    Rupp, B.5
  • 22
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • W. Minor, M. Cymborowski, Z. Otwinowski, and M. Chruszcz HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr D Biol Crystallogr 62 2006 859 866
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 24
    • 84891668860 scopus 로고    scopus 로고
    • Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server
    • H. Zheng, M.D. Chordia, D.R. Cooper, M. Chruszcz, P. Muller, G.M. Sheldrick, and et al. Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server Nat Protoc 9 2014 156 170
    • (2014) Nat Protoc , vol.9 , pp. 156-170
    • Zheng, H.1    Chordia, M.D.2    Cooper, D.R.3    Chruszcz, M.4    Muller, P.5    Sheldrick, G.M.6
  • 26
    • 0032033678 scopus 로고    scopus 로고
    • Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • C.A. Scott, P.A. Peterson, L. Teyton, and I.A. Wilson Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues Immunity 8 1998 319 329
    • (1998) Immunity , vol.8 , pp. 319-329
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 27
    • 84905496084 scopus 로고    scopus 로고
    • Structural basis for the specific recognition of the major antigenic peptide from the Japanese cedar pollen allergen Cry j 1 by HLA-DP5
    • S. Kusano, M. Kukimoto-Niino, Y. Satta, N. Ohsawa, T. Uchikubo-Kamo, M. Wakiyama, and et al. Structural basis for the specific recognition of the major antigenic peptide from the Japanese cedar pollen allergen Cry j 1 by HLA-DP5 J Mol Biol 426 2014 3016 3027
    • (2014) J Mol Biol , vol.426 , pp. 3016-3027
    • Kusano, S.1    Kukimoto-Niino, M.2    Satta, Y.3    Ohsawa, N.4    Uchikubo-Kamo, T.5    Wakiyama, M.6
  • 28
    • 38649137731 scopus 로고    scopus 로고
    • Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system
    • S.L. LaPorte, Z.S. Juo, J. Vaclavikova, L.A. Colf, X. Qi, N.M. Heller, and et al. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system Cell 132 2008 259 272
    • (2008) Cell , vol.132 , pp. 259-272
    • Laporte, S.L.1    Juo, Z.S.2    Vaclavikova, J.3    Colf, L.A.4    Qi, X.5    Heller, N.M.6
  • 29
    • 84897412926 scopus 로고    scopus 로고
    • A molecular perspective on TH2-promoting cytokine receptors in patients with allergic disease
    • M.J. Romeo, R. Agrawal, A. Pomés, and J.A. Woodfolk A molecular perspective on TH2-promoting cytokine receptors in patients with allergic disease J Allergy Clin Immunol 133 2014 952 960
    • (2014) J Allergy Clin Immunol , vol.133 , pp. 952-960
    • Romeo, M.J.1    Agrawal, R.2    Pomés, A.3    Woodfolk, J.A.4
  • 30
    • 79955603056 scopus 로고    scopus 로고
    • Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcεRI
    • M.D. Holdom, A.M. Davies, J.E. Nettleship, S.C. Bagby, B. Dhaliwal, E. Girardi, and et al. Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcεRI Nat Struct Mol Biol 18 2011 571 576
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 571-576
    • Holdom, M.D.1    Davies, A.M.2    Nettleship, J.E.3    Bagby, S.C.4    Dhaliwal, B.5    Girardi, E.6
  • 32
    • 84881233799 scopus 로고    scopus 로고
    • Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin e
    • D. Yuan, A.H. Keeble, R.G. Hibbert, S. Fabiane, H.J. Gould, J.M. McDonnell, and et al. Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin E J Biol Chem 288 2013 21667 21677
    • (2013) J Biol Chem , vol.288 , pp. 21667-21677
    • Yuan, D.1    Keeble, A.H.2    Hibbert, R.G.3    Fabiane, S.4    Gould, H.J.5    McDonnell, J.M.6
  • 33
    • 84864497135 scopus 로고    scopus 로고
    • Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor FcepsilonRI
    • B. Dhaliwal, D. Yuan, M.O. Pang, A.J. Henry, K. Cain, A. Oxbrow, and et al. Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor FcepsilonRI Proc Natl Acad Sci U S A 109 2012 12686 12691
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 12686-12691
    • Dhaliwal, B.1    Yuan, D.2    Pang, M.O.3    Henry, A.J.4    Cain, K.5    Oxbrow, A.6
  • 34
    • 79953890803 scopus 로고    scopus 로고
    • The structural biology of Toll-like receptors
    • I. Botos, D.M. Segal, and D.R. Davies The structural biology of Toll-like receptors Structure 19 2011 447 459
    • (2011) Structure , vol.19 , pp. 447-459
    • Botos, I.1    Segal, D.M.2    Davies, D.R.3
  • 35
    • 0026475945 scopus 로고
    • Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
    • Z. Bocskei, C.R. Groom, D.R. Flower, C.E. Wright, S.E. Phillips, A. Cavaggioni, and et al. Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography Nature 360 1992 186 188
    • (1992) Nature , vol.360 , pp. 186-188
    • Bocskei, Z.1    Groom, C.R.2    Flower, D.R.3    Wright, C.E.4    Phillips, S.E.5    Cavaggioni, A.6
  • 37
    • 84937000024 scopus 로고    scopus 로고
    • Early childhood IgE reactivity to pathogenesis-related class 10 proteins predicts allergic rhinitis in adolescence
    • M. Westman, C. Lupinek, J. Bousquet, N. Andersson, S. Pahr, A. Baar, and et al. Early childhood IgE reactivity to pathogenesis-related class 10 proteins predicts allergic rhinitis in adolescence J Allergy Clin Immunol 135 2015 1199 1206.e11
    • (2015) J Allergy Clin Immunol , vol.135 , pp. 1199-1206e11
    • Westman, M.1    Lupinek, C.2    Bousquet, J.3    Andersson, N.4    Pahr, S.5    Baar, A.6
  • 39
    • 84895510145 scopus 로고    scopus 로고
    • Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences
    • C. Radauer, A. Nandy, F. Ferreira, R.E. Goodman, J.N. Larsen, J. Lidholm, and et al. Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences Allergy 69 2014 413 419
    • (2014) Allergy , vol.69 , pp. 413-419
    • Radauer, C.1    Nandy, A.2    Ferreira, F.3    Goodman, R.E.4    Larsen, J.N.5    Lidholm, J.6
  • 40
    • 38149102307 scopus 로고    scopus 로고
    • Naturally occurring hypoallergenic Bet v 1 isoforms fail to induce IgE responses in individuals with birch pollen allergy
    • S. Wagner, C. Radauer, M. Bublin, K. Hoffmann-Sommergruber, T. Kopp, E.K. Greisenegger, and et al. Naturally occurring hypoallergenic Bet v 1 isoforms fail to induce IgE responses in individuals with birch pollen allergy J Allergy Clin Immunol 121 2008 246 252
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 246-252
    • Wagner, S.1    Radauer, C.2    Bublin, M.3    Hoffmann-Sommergruber, K.4    Kopp, T.5    Greisenegger, E.K.6
  • 42
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • C. Radauer, M. Bublin, S. Wagner, A. Mari, and H. Breiteneder Allergens are distributed into few protein families and possess a restricted number of biochemical functions J Allergy Clin Immunol 121 2008 847 852
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 847-852
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5
  • 44
    • 56849119061 scopus 로고    scopus 로고
    • Annotating proteins with generalized functional linkages
    • R. Llewellyn, and D.S. Eisenberg Annotating proteins with generalized functional linkages Proc Natl Acad Sci U S A 105 2008 17700 17705
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17700-17705
    • Llewellyn, R.1    Eisenberg, D.S.2
  • 46
    • 59349114360 scopus 로고    scopus 로고
    • Crystal structures of mite allergens der f 1 and der p 1 reveal differences in surface-exposed residues that may influence antibody binding
    • M. Chruszcz, M.D. Chapman, L.D. Vailes, E.A. Stura, J.M. Saint-Remy, W. Minor, and et al. Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding J Mol Biol 386 2009 520 530
    • (2009) J Mol Biol , vol.386 , pp. 520-530
    • Chruszcz, M.1    Chapman, M.D.2    Vailes, L.D.3    Stura, E.A.4    Saint-Remy, J.M.5    Minor, W.6
  • 47
    • 84857711026 scopus 로고    scopus 로고
    • Molecular determinants for antibody binding on group 1 house dust mite allergens
    • M. Chruszcz, A. Pomés, J. Glesner, L.D. Vailes, T. Osinski, P.J. Porebski, and et al. Molecular determinants for antibody binding on group 1 house dust mite allergens J Biol Chem 287 2012 7388 7398
    • (2012) J Biol Chem , vol.287 , pp. 7388-7398
    • Chruszcz, M.1    Pomés, A.2    Glesner, J.3    Vailes, L.D.4    Osinski, T.5    Porebski, P.J.6
  • 48
  • 49
    • 16244384649 scopus 로고    scopus 로고
    • Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition
    • A. Gustchina, M. Li, S. Wünschmann, M.D. Chapman, A. Pomés, and A. Wlodawer Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition J Mol Biol 348 2005 433 444
    • (2005) J Mol Biol , vol.348 , pp. 433-444
    • Gustchina, A.1    Li, M.2    Wünschmann, S.3    Chapman, M.D.4    Pomés, A.5    Wlodawer, A.6
  • 51
    • 0036791736 scopus 로고    scopus 로고
    • The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly
    • P. Verdino, K. Westritschnig, R. Valenta, and W. Keller The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly EMBO J 21 2002 5007 5016
    • (2002) EMBO J , vol.21 , pp. 5007-5016
    • Verdino, P.1    Westritschnig, K.2    Valenta, R.3    Keller, W.4
  • 52
    • 80655128132 scopus 로고    scopus 로고
    • Structural and immunologic characterization of Ara h 1, a major peanut allergen
    • M. Chruszcz, S.J. Maleki, K.A. Majorek, M. Demas, M. Bublin, R. Solberg, and et al. Structural and immunologic characterization of Ara h 1, a major peanut allergen J Biol Chem 286 2011 39318 39327
    • (2011) J Biol Chem , vol.286 , pp. 39318-39327
    • Chruszcz, M.1    Maleki, S.J.2    Majorek, K.A.3    Demas, M.4    Bublin, M.5    Solberg, R.6
  • 53
    • 0034120710 scopus 로고    scopus 로고
    • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation
    • S.J. Maleki, R.A. Kopper, D.S. Shin, C.W. Park, C.M. Compadre, H. Sampson, and et al. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation J Immunol 164 2000 5844 5849
    • (2000) J Immunol , vol.164 , pp. 5844-5849
    • Maleki, S.J.1    Kopper, R.A.2    Shin, D.S.3    Park, C.W.4    Compadre, C.M.5    Sampson, H.6
  • 54
    • 79952307950 scopus 로고    scopus 로고
    • Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy
    • N. Nicolaou, C. Murray, D. Belgrave, M. Poorafshar, A. Simpson, and A. Custovic Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy J Allergy Clin Immunol 127 2011 684 685
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 684-685
    • Nicolaou, N.1    Murray, C.2    Belgrave, D.3    Poorafshar, M.4    Simpson, A.5    Custovic, A.6
  • 57
    • 84862894294 scopus 로고    scopus 로고
    • Alternaria alternata allergen Alt a 1: A unique beta-barrel protein dimer found exclusively in fungi
    • M. Chruszcz, M.D. Chapman, T. Osinski, R. Solberg, M. Demas, P.J. Porebski, and et al. Alternaria alternata allergen Alt a 1: a unique beta-barrel protein dimer found exclusively in fungi J Allergy Clin Immunol 130 2012 241 247
    • (2012) J Allergy Clin Immunol , vol.130 , pp. 241-247
    • Chruszcz, M.1    Chapman, M.D.2    Osinski, T.3    Solberg, R.4    Demas, M.5    Porebski, P.J.6
  • 58
    • 84892557258 scopus 로고    scopus 로고
    • Genomic, RNAseq, and molecular modeling evidence suggests that the major allergen domain in insects evolved from a homodimeric origin
    • T.A. Randall, L. Perera, R.E. London, and G.A. Mueller Genomic, RNAseq, and molecular modeling evidence suggests that the major allergen domain in insects evolved from a homodimeric origin Genome Biol Evol 5 2013 2344 2358
    • (2013) Genome Biol Evol , vol.5 , pp. 2344-2358
    • Randall, T.A.1    Perera, L.2    London, R.E.3    Mueller, G.A.4
  • 60
    • 0141844497 scopus 로고    scopus 로고
    • The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family
    • L. Kaiser, H. Gronlund, T. Sandalova, H.G. Ljunggren, M. van Hage-Hamsten, A. Achour, and et al. The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family J Biol Chem 278 2003 37730 37735
    • (2003) J Biol Chem , vol.278 , pp. 37730-37735
    • Kaiser, L.1    Gronlund, H.2    Sandalova, T.3    Ljunggren, H.G.4    Van Hage-Hamsten, M.5    Achour, A.6
  • 62
    • 0036307905 scopus 로고    scopus 로고
    • The crystal structure of a major dust mite allergen der p 2, and its biological implications
    • U. Derewenda, J. Li, Z. Derewenda, Z. Dauter, G.A. Mueller, G.S. Rule, and et al. The crystal structure of a major dust mite allergen Der p 2, and its biological implications J Mol Biol 318 2002 189 197
    • (2002) J Mol Biol , vol.318 , pp. 189-197
    • Derewenda, U.1    Li, J.2    Derewenda, Z.3    Dauter, Z.4    Mueller, G.A.5    Rule, G.S.6
  • 63
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • B.S. Park, D.H. Song, H.M. Kim, B.S. Choi, H. Lee, and J.O. Lee The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex Nature 458 2009 1191 1195
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5    Lee, J.O.6
  • 64
    • 59049100417 scopus 로고    scopus 로고
    • Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein
    • A. Trompette, S. Divanovic, A. Visintin, C. Blanchard, R.S. Hegde, R. Madan, and et al. Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein Nature 457 2009 585 588
    • (2009) Nature , vol.457 , pp. 585-588
    • Trompette, A.1    Divanovic, S.2    Visintin, A.3    Blanchard, C.4    Hegde, R.S.5    Madan, R.6
  • 65
    • 77951665783 scopus 로고    scopus 로고
    • Guilt by intimate association: What makes an allergen an allergen?
    • C.L. Karp Guilt by intimate association: what makes an allergen an allergen? J Allergy Clin Immunol 125 2010 955 960
    • (2010) J Allergy Clin Immunol , vol.125 , pp. 955-960
    • Karp, C.L.1
  • 66
    • 0037121946 scopus 로고    scopus 로고
    • Lipopolysaccharide-enhanced, toll-like receptor 4-dependent T helper cell type 2 responses to inhaled antigen
    • S.C. Eisenbarth, D.A. Piggott, J.W. Huleatt, I. Visintin, C.A. Herrick, and K. Bottomly Lipopolysaccharide-enhanced, toll-like receptor 4-dependent T helper cell type 2 responses to inhaled antigen J Exp Med 196 2002 1645 1651
    • (2002) J Exp Med , vol.196 , pp. 1645-1651
    • Eisenbarth, S.C.1    Piggott, D.A.2    Huleatt, J.W.3    Visintin, I.4    Herrick, C.A.5    Bottomly, K.6
  • 68
    • 1342324768 scopus 로고    scopus 로고
    • Cutting edge: Activation of Toll-like receptor 2 induces a Th2 immune response and promotes experimental asthma
    • V. Redecke, H. Hacker, S.K. Datta, A. Fermin, P.M. Pitha, D.H. Broide, and et al. Cutting edge: activation of Toll-like receptor 2 induces a Th2 immune response and promotes experimental asthma J Immunol 172 2004 2739 2743
    • (2004) J Immunol , vol.172 , pp. 2739-2743
    • Redecke, V.1    Hacker, H.2    Datta, S.K.3    Fermin, A.4    Pitha, P.M.5    Broide, D.H.6
  • 71
    • 0028871972 scopus 로고
    • Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23)
    • O. Schulz, P. Laing, H.F. Sewell, and F. Shakib Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23) Eur J Immunol 25 1995 3191 3194
    • (1995) Eur J Immunol , vol.25 , pp. 3191-3194
    • Schulz, O.1    Laing, P.2    Sewell, H.F.3    Shakib, F.4
  • 72
    • 0028818335 scopus 로고
    • A major house dust mite allergen disrupts the immunoglobulin e network by selectively cleaving CD23: Innate protection by antiproteases
    • C.R. Hewitt, A.P. Brown, B.J. Hart, and D.I. Pritchard A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases J Exp Med 182 1995 1537 1544
    • (1995) J Exp Med , vol.182 , pp. 1537-1544
    • Hewitt, C.R.1    Brown, A.P.2    Hart, B.J.3    Pritchard, D.I.4
  • 73
    • 0032193198 scopus 로고    scopus 로고
    • Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium
    • C. King, S. Brennan, P.J. Thompson, and G.A. Stewart Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium J Immunol 161 1998 3645 3651
    • (1998) J Immunol , vol.161 , pp. 3645-3651
    • King, C.1    Brennan, S.2    Thompson, P.J.3    Stewart, G.A.4
  • 74
    • 0032695151 scopus 로고    scopus 로고
    • Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions
    • H. Wan, H.L. Winton, C. Soeller, E.R. Tovey, D.C. Gruenert, P.J. Thompson, and et al. Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions J Clin Invest 104 1999 123 133
    • (1999) J Clin Invest , vol.104 , pp. 123-133
    • Wan, H.1    Winton, H.L.2    Soeller, C.3    Tovey, E.R.4    Gruenert, D.C.5    Thompson, P.J.6
  • 76
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • D.R. Flower The lipocalin protein family: structure and function Biochem J 318 1996 1 14
    • (1996) Biochem J , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 77
    • 84889797970 scopus 로고    scopus 로고
    • The structure of latherin, a surfactant allergen protein from horse sweat and saliva
    • S.J. Vance, R.E. McDonald, A. Cooper, B.O. Smith, and M.W. Kennedy The structure of latherin, a surfactant allergen protein from horse sweat and saliva J R Soc Interface 10 2013 20130453
    • (2013) J R Soc Interface , vol.10 , pp. 20130453
    • Vance, S.J.1    McDonald, R.E.2    Cooper, A.3    Smith, B.O.4    Kennedy, M.W.5
  • 78
    • 84906944486 scopus 로고    scopus 로고
    • Do lipids influence the allergic sensitization process?
    • M. Bublin, T. Eiwegger, and H. Breiteneder Do lipids influence the allergic sensitization process? J Allergy Clin Immunol 134 2014 521 529
    • (2014) J Allergy Clin Immunol , vol.134 , pp. 521-529
    • Bublin, M.1    Eiwegger, T.2    Breiteneder, H.3
  • 79
    • 33745156067 scopus 로고    scopus 로고
    • Randomized double-blind controlled study with sublingual carbamylated allergoid immunotherapy in mild rhinitis due to mites
    • G. Passalacqua, M. Pasquali, R. Ariano, C. Lombardi, A. Giardini, I. Baiardini, and et al. Randomized double-blind controlled study with sublingual carbamylated allergoid immunotherapy in mild rhinitis due to mites Allergy 61 2006 849 854
    • (2006) Allergy , vol.61 , pp. 849-854
    • Passalacqua, G.1    Pasquali, M.2    Ariano, R.3    Lombardi, C.4    Giardini, A.5    Baiardini, I.6
  • 80
    • 79953650923 scopus 로고    scopus 로고
    • Recombinant allergens for specific immunotherapy
    • O. Cromwell, D. Hafner, and A. Nandy Recombinant allergens for specific immunotherapy J Allergy Clin Immunol 127 2011 865 872
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 865-872
    • Cromwell, O.1    Hafner, D.2    Nandy, A.3
  • 81
    • 84878090456 scopus 로고    scopus 로고
    • Double-blind, placebo-controlled, dose-ranging study of new recombinant hypoallergenic Bet v 1 in an environmental exposure chamber
    • W. Meyer, A. Narkus, A.M. Salapatek, and D. Hafner Double-blind, placebo-controlled, dose-ranging study of new recombinant hypoallergenic Bet v 1 in an environmental exposure chamber Allergy 68 2013 724 731
    • (2013) Allergy , vol.68 , pp. 724-731
    • Meyer, W.1    Narkus, A.2    Salapatek, A.M.3    Hafner, D.4
  • 82
    • 0031921016 scopus 로고    scopus 로고
    • Recombinant allergens for immunotherapy: A der p 2 variant with reduced IgE reactivity retains T-cell epitopes
    • A.M. Smith, M.D. Chapman, E.A. Taketomi, T.A. Platts-Mills, and S.S. Sung Recombinant allergens for immunotherapy: a Der p 2 variant with reduced IgE reactivity retains T-cell epitopes J Allergy Clin Immunol 101 1998 423 425
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 423-425
    • Smith, A.M.1    Chapman, M.D.2    Taketomi, E.A.3    Platts-Mills, T.A.4    Sung, S.S.5
  • 83
    • 0030854098 scopus 로고    scopus 로고
    • Engineering of the major house dust mite allergen der f 2 for allergen-specific immunotherapy
    • T. Takai, T. Yokota, M. Yasue, C. Nishiyama, T. Yuuki, A. Mori, and et al. Engineering of the major house dust mite allergen Der f 2 for allergen-specific immunotherapy Nat Biotechnol 15 1997 754 758
    • (1997) Nat Biotechnol , vol.15 , pp. 754-758
    • Takai, T.1    Yokota, T.2    Yasue, M.3    Nishiyama, C.4    Yuuki, T.5    Mori, A.6
  • 84
    • 0034235234 scopus 로고    scopus 로고
    • Dominant epitopes and allergic cross-reactivity: Complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1
    • O. Mirza, A. Henriksen, H. Ipsen, J.N. Larsen, M. Wissenbach, M.D. Spangfort, and et al. Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1 J Immunol 165 2000 331 338
    • (2000) J Immunol , vol.165 , pp. 331-338
    • Mirza, O.1    Henriksen, A.2    Ipsen, H.3    Larsen, J.N.4    Wissenbach, M.5    Spangfort, M.D.6
  • 85
    • 0041385755 scopus 로고    scopus 로고
    • Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis
    • M.D. Spangfort, O. Mirza, H. Ipsen, R.J. Van Neerven, M. Gajhede, and J.N. Larsen Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis J Immunol 171 2003 3084 3090
    • (2003) J Immunol , vol.171 , pp. 3084-3090
    • Spangfort, M.D.1    Mirza, O.2    Ipsen, H.3    Van Neerven, R.J.4    Gajhede, M.5    Larsen, J.N.6
  • 86
    • 34047171268 scopus 로고    scopus 로고
    • Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab
    • S. Padavattan, T. Schirmer, M. Schmidt, C. Akdis, R. Valenta, I. Mittermann, and et al. Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab J Mol Biol 368 2007 742 752
    • (2007) J Mol Biol , vol.368 , pp. 742-752
    • Padavattan, S.1    Schirmer, T.2    Schmidt, M.3    Akdis, C.4    Valenta, R.5    Mittermann, I.6
  • 87
    • 35748953107 scopus 로고    scopus 로고
    • Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen
    • M. Niemi, S. Jylha, M.L. Laukkanen, H. Soderlund, S. Makinen-Kiljunen, J.M. Kallio, and et al. Molecular interactions between a recombinant IgE antibody and the beta-lactoglobulin allergen Structure 15 2007 1413 1421
    • (2007) Structure , vol.15 , pp. 1413-1421
    • Niemi, M.1    Jylha, S.2    Laukkanen, M.L.3    Soderlund, H.4    Makinen-Kiljunen, S.5    Kallio, J.M.6
  • 88
    • 61449212919 scopus 로고    scopus 로고
    • High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography
    • S. Padavattan, S. Flicker, T. Schirmer, C. Madritsch, S. Randow, G. Reese, and et al. High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography J Immunol 182 2009 2141 2151
    • (2009) J Immunol , vol.182 , pp. 2141-2151
    • Padavattan, S.1    Flicker, S.2    Schirmer, T.3    Madritsch, C.4    Randow, S.5    Reese, G.6
  • 89
    • 53049108650 scopus 로고    scopus 로고
    • Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody
    • M. Li, A. Gustchina, J. Alexandratos, A. Wlodawer, S. Wunschmann, C.L. Kepley, and et al. Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody J Biol Chem 283 2008 22806 22814
    • (2008) J Biol Chem , vol.283 , pp. 22806-22814
    • Li, M.1    Gustchina, A.2    Alexandratos, J.3    Wlodawer, A.4    Wunschmann, S.5    Kepley, C.L.6
  • 90
    • 79251583126 scopus 로고    scopus 로고
    • Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody
    • M. Li, A. Gustchina, J. Glesner, S. Wunschmann, L.D. Vailes, M.D. Chapman, and et al. Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody J Immunol 186 2011 333 340
    • (2011) J Immunol , vol.186 , pp. 333-340
    • Li, M.1    Gustchina, A.2    Glesner, J.3    Wunschmann, S.4    Vailes, L.D.5    Chapman, M.D.6
  • 91
    • 84932090487 scopus 로고    scopus 로고
    • Structural analysis of der p 1-antibody complexes and comparison with complexes of proteins or peptides with monoclonal antibodies
    • In press
    • T. Osinski, A. Pomés, K.A. Majorek, J. Glesner, L.R. Offermann, L.D. Vailes, and et al. Structural analysis of Der p 1-antibody complexes and comparison with complexes of proteins or peptides with monoclonal antibodies J Immunol 2015 In press
    • (2015) J Immunol
    • Osinski, T.1    Pomés, A.2    Majorek, K.A.3    Glesner, J.4    Offermann, L.R.5    Vailes, L.D.6
  • 92
    • 79960301160 scopus 로고    scopus 로고
    • Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding
    • J. Glesner, S. Wunschmann, M. Li, A. Gustchina, A. Wlodawer, M. Himly, and et al. Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding PLoS One 6 2011 e22223
    • (2011) PLoS One , vol.6 , pp. e22223
    • Glesner, J.1    Wunschmann, S.2    Li, M.3    Gustchina, A.4    Wlodawer, A.5    Himly, M.6
  • 93
    • 84859737960 scopus 로고    scopus 로고
    • How molecular diagnosis can change allergen-specific immunotherapy prescription in a complex pollen area
    • J. Sastre, M.E. Landivar, M. Ruiz-Garcia, M.V. Andregnette-Rosigno, and I. Mahillo How molecular diagnosis can change allergen-specific immunotherapy prescription in a complex pollen area Allergy 67 2012 709 711
    • (2012) Allergy , vol.67 , pp. 709-711
    • Sastre, J.1    Landivar, M.E.2    Ruiz-Garcia, M.3    Andregnette-Rosigno, M.V.4    Mahillo, I.5
  • 94
    • 84903748177 scopus 로고    scopus 로고
    • The effect of component-resolved diagnosis on specific immunotherapy prescription in children with hay fever
    • G. Stringari, S. Tripodi, C. Caffarelli, A. Dondi, R. Asero, B.A. Di Rienzo, and et al. The effect of component-resolved diagnosis on specific immunotherapy prescription in children with hay fever J Allergy Clin Immunol 134 2014 75 81
    • (2014) J Allergy Clin Immunol , vol.134 , pp. 75-81
    • Stringari, G.1    Tripodi, S.2    Caffarelli, C.3    Dondi, A.4    Asero, R.5    Di Rienzo, B.A.6
  • 95
    • 84857801459 scopus 로고    scopus 로고
    • Molecular profiles of IgE to Phleum pratense in children with grass pollen allergy: Implications for specific immunotherapy
    • S. Tripodi, T. Frediani, S. Lucarelli, F. Macri, G. Pingitore, B.A. Di Rienzo, and et al. Molecular profiles of IgE to Phleum pratense in children with grass pollen allergy: implications for specific immunotherapy J Allergy Clin Immunol 129 2012 834 839
    • (2012) J Allergy Clin Immunol , vol.129 , pp. 834-839
    • Tripodi, S.1    Frediani, T.2    Lucarelli, S.3    Macri, F.4    Pingitore, G.5    Di Rienzo, B.A.6
  • 96
  • 98
    • 30744466669 scopus 로고    scopus 로고
    • Structural features of allergenic molecules
    • R.C. Aalberse Structural features of allergenic molecules Chem Immunol Allergy 91 2006 134 146
    • (2006) Chem Immunol Allergy , vol.91 , pp. 134-146
    • Aalberse, R.C.1
  • 99
    • 84897827623 scopus 로고    scopus 로고
    • Goat's milk allergy without cow's milk allergy: Suppression of non-cross-reactive epitopes on caprine beta-casein
    • S. Hazebrouck, S. Ah-Leung, E. Bidat, E. Paty, M.F. Drumare, S. Tilleul, and et al. Goat's milk allergy without cow's milk allergy: suppression of non-cross-reactive epitopes on caprine beta-casein Clin Exp Allergy 44 2014 602 610
    • (2014) Clin Exp Allergy , vol.44 , pp. 602-610
    • Hazebrouck, S.1    Ah-Leung, S.2    Bidat, E.3    Paty, E.4    Drumare, M.F.5    Tilleul, S.6
  • 101
    • 79958138380 scopus 로고    scopus 로고
    • Kiwifruit Act d 11 is the first member of the ripening-related protein family identified as an allergen
    • R. D'Avino, M.L. Bernardi, M. Wallner, P. Palazzo, L. Camardella, L. Tuppo, and et al. Kiwifruit Act d 11 is the first member of the ripening-related protein family identified as an allergen Allergy 66 2011 870 877
    • (2011) Allergy , vol.66 , pp. 870-877
    • D'Avino, R.1    Bernardi, M.L.2    Wallner, M.3    Palazzo, P.4    Camardella, L.5    Tuppo, L.6
  • 102
    • 84882862050 scopus 로고    scopus 로고
    • IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3
    • M. Bublin, M. Kostadinova, C. Radauer, C. Hafner, Z. Szepfalusi, E.M. Varga, and et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3 J Allergy Clin Immunol 132 2013 118 124
    • (2013) J Allergy Clin Immunol , vol.132 , pp. 118-124
    • Bublin, M.1    Kostadinova, M.2    Radauer, C.3    Hafner, C.4    Szepfalusi, Z.5    Varga, E.M.6
  • 103
    • 84874805505 scopus 로고    scopus 로고
    • Assessment of 3D models for allergen research
    • T.D. Power, O. Ivanciuc, C.H. Schein, and W. Braun Assessment of 3D models for allergen research Proteins 81 2013 545 554
    • (2013) Proteins , vol.81 , pp. 545-554
    • Power, T.D.1    Ivanciuc, O.2    Schein, C.H.3    Braun, W.4
  • 104
    • 0034995912 scopus 로고    scopus 로고
    • Cross-reactivity of IgE antibodies to allergens
    • R.C. Aalberse, J. Akkerdaas, and R. van Ree Cross-reactivity of IgE antibodies to allergens Allergy 56 2001 478 490
    • (2001) Allergy , vol.56 , pp. 478-490
    • Aalberse, R.C.1    Akkerdaas, J.2    Van Ree, R.3
  • 105
    • 84928562385 scopus 로고    scopus 로고
    • Analysis of glutathione S-transferase allergen cross-reactivity in a North American population: Relevance for molecular diagnosis
    • 140-50, e1-7
    • G.A. Mueller, L.C. Pedersen, J. Glesner, L.L. Edwards, J. Zakzuk, R.E. London, and et al. Analysis of glutathione S-transferase allergen cross-reactivity in a North American population: relevance for molecular diagnosis J Allergy Clin Immunol 136 2015 140-50, e1-7
    • (2015) J Allergy Clin Immunol , vol.136
    • Mueller, G.A.1    Pedersen, L.C.2    Glesner, J.3    Edwards, L.L.4    Zakzuk, J.5    London, R.E.6
  • 106
    • 84906087743 scopus 로고    scopus 로고
    • Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser
    • C. Kupitz, S. Basu, I. Grotjohann, R. Fromme, N.A. Zatsepin, K.N. Rendek, and et al. Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser Nature 513 2014 261 265
    • (2014) Nature , vol.513 , pp. 261-265
    • Kupitz, C.1    Basu, S.2    Grotjohann, I.3    Fromme, R.4    Zatsepin, N.A.5    Rendek, K.N.6
  • 107
    • 84893352313 scopus 로고    scopus 로고
    • Crystallography: Sources of inspiration
    • S. McSweeney, and P. Fromme Crystallography: sources of inspiration Nature 505 2014 620 621
    • (2014) Nature , vol.505 , pp. 620-621
    • McSweeney, S.1    Fromme, P.2
  • 109
    • 84895510145 scopus 로고    scopus 로고
    • Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences
    • C. Radauer, A. Nandy, F. Ferreira, R.E. Goodman, J.N. Larsen, J. Lidholm, and et al. Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences Allergy 69 2014 413 419
    • (2014) Allergy , vol.69 , pp. 413-419
    • Radauer, C.1    Nandy, A.2    Ferreira, F.3    Goodman, R.E.4    Larsen, J.N.5    Lidholm, J.6
  • 110
    • 84857711026 scopus 로고    scopus 로고
    • Molecular determinants for antibody binding on group 1 house dust mite allergens
    • M. Chruszcz, A. Pomés, J. Glesner, L.D. Vailes, T. Osinski, P.J. Porebski, and et al. Molecular determinants for antibody binding on group 1 house dust mite allergens J Biol Chem 287 2012 7388 7398
    • (2012) J Biol Chem , vol.287 , pp. 7388-7398
    • Chruszcz, M.1    Pomés, A.2    Glesner, J.3    Vailes, L.D.4    Osinski, T.5    Porebski, P.J.6
  • 111
    • 16244384649 scopus 로고    scopus 로고
    • Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition
    • A. Gustchina, M. Li, S. Wünschmann, M.D. Chapman, A. Pomés, and A. Wlodawer Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition J Mol Biol 348 2005 433 444
    • (2005) J Mol Biol , vol.348 , pp. 433-444
    • Gustchina, A.1    Li, M.2    Wünschmann, S.3    Chapman, M.D.4    Pomés, A.5    Wlodawer, A.6
  • 112
    • 24744439695 scopus 로고    scopus 로고
    • The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen
    • K. Meno, P.B. Thorsted, H. Ipsen, O. Kristensen, J.N. Larsen, M.D. Spangfort, and et al. The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen J Immunol 175 2005 3835 3845
    • (2005) J Immunol , vol.175 , pp. 3835-3845
    • Meno, K.1    Thorsted, P.B.2    Ipsen, H.3    Kristensen, O.4    Larsen, J.N.5    Spangfort, M.D.6
  • 113
    • 33644777433 scopus 로고    scopus 로고
    • Three-dimensional structure and IgE-binding properties of mature fully active der p 1, a clinically relevant major allergen
    • S. de Halleux, E. Stura, L. VanderElst, V. Carlier, M. Jacquemin, and J.M. Saint-Remy Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen J Allergy Clin Immunol 117 2006 571 576
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 571-576
    • De Halleux, S.1    Stura, E.2    Vanderelst, L.3    Carlier, V.4    Jacquemin, M.5    Saint-Remy, J.M.6
  • 114
    • 85059207143 scopus 로고    scopus 로고
    • Structural analysis reveals molecular basis for interactions of group 1 allergens with species specific and cross-reactive antibodies
    • M. Chruszcz, A. Pomés, T. Osinski, K.A. Majorek, J. Glesner, W. Minor, and et al. Structural analysis reveals molecular basis for interactions of group 1 allergens with species specific and cross-reactive antibodies J Allergy Clin Immunol 131 2013 AB15
    • (2013) J Allergy Clin Immunol , vol.131 , pp. AB15
    • Chruszcz, M.1    Pomés, A.2    Osinski, T.3    Majorek, K.A.4    Glesner, J.5    Minor, W.6
  • 115
    • 0032515169 scopus 로고    scopus 로고
    • Novel allergen structures with tandem amino acid repeats derived from German and American cockroach
    • A. Pomés, E. Melén, L.D. Vailes, J.D. Retief, L.K. Arruda, and M.D. Chapman Novel allergen structures with tandem amino acid repeats derived from German and American cockroach J Biol Chem 273 1998 30801 30807
    • (1998) J Biol Chem , vol.273 , pp. 30801-30807
    • Pomés, A.1    Melén, E.2    Vailes, L.D.3    Retief, J.D.4    Arruda, L.K.5    Chapman, M.D.6
  • 116
    • 85028094245 scopus 로고    scopus 로고
    • The novel structure of the cockroach allergen Bla g 1 has implications for allergenicity and exposure assessment
    • G.A. Mueller, L.C. Pedersen, F.B. Lih, J. Glesner, A.F. Moon, M.D. Chapman, and et al. The novel structure of the cockroach allergen Bla g 1 has implications for allergenicity and exposure assessment J Allergy Clin Immunol 132 2013 1420 1426
    • (2013) J Allergy Clin Immunol , vol.132 , pp. 1420-1426
    • Mueller, G.A.1    Pedersen, L.C.2    Lih, F.B.3    Glesner, J.4    Moon, A.F.5    Chapman, M.D.6
  • 117
    • 0036307905 scopus 로고    scopus 로고
    • The crystal structure of a major dust mite allergen der p 2, and its biological implications
    • U. Derewenda, J. Li, Z. Derewenda, Z. Dauter, G.A. Mueller, G.S. Rule, and et al. The crystal structure of a major dust mite allergen Der p 2, and its biological implications J Mol Biol 318 2002 189 197
    • (2002) J Mol Biol , vol.318 , pp. 189-197
    • Derewenda, U.1    Li, J.2    Derewenda, Z.3    Dauter, Z.4    Mueller, G.A.5    Rule, G.S.6
  • 118
    • 0028083231 scopus 로고
    • Effects of amino acid variations in recombinant der fII on its human IgE and mouse IgG recognition
    • C. Nishiyama, T. Yuuki, Y. Usui, N. Iwamoto, Y. Okumura, and H. Okudaira Effects of amino acid variations in recombinant Der fII on its human IgE and mouse IgG recognition Int Arch Allergy Immunol 105 1994 62 69
    • (1994) Int Arch Allergy Immunol , vol.105 , pp. 62-69
    • Nishiyama, C.1    Yuuki, T.2    Usui, Y.3    Iwamoto, N.4    Okumura, Y.5    Okudaira, H.6
  • 120
    • 79958149376 scopus 로고    scopus 로고
    • Ara h 2: Crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity
    • G.A. Mueller, R.A. Gosavi, A. Pomés, S. Wunschmann, A.F. Moon, R.E. London, and et al. Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity Allergy 66 2011 878 885
    • (2011) Allergy , vol.66 , pp. 878-885
    • Mueller, G.A.1    Gosavi, R.A.2    Pomés, A.3    Wunschmann, S.4    Moon, A.F.5    London, R.E.6
  • 121
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Z.S. Derewenda Rational protein crystallization by mutational surface engineering Structure 12 2004 529 535
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 122
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP): A reporter of gene expression in Candida albicans
    • B.P. Cormack, G. Bertram, M. Egerton, N.A. Gow, S. Falkow, and A.J. Brown Yeast-enhanced green fluorescent protein (yEGFP): a reporter of gene expression in Candida albicans Microbiology 143 1997 303 311
    • (1997) Microbiology , vol.143 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.4    Falkow, S.5    Brown, A.J.6
  • 125
    • 84872594543 scopus 로고    scopus 로고
    • Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg2+-bound, and fully Ca2+-bound
    • M.T. Henzl, A.G. Sirianni, W.G. Wycoff, A. Tan, and J.J. Tanner Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg2+-bound, and fully Ca2+-bound Proteins 81 2013 300 315
    • (2013) Proteins , vol.81 , pp. 300-315
    • Henzl, M.T.1    Sirianni, A.G.2    Wycoff, W.G.3    Tan, A.4    Tanner, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.