메뉴 건너뛰기




Volumn 157, Issue 11, 1996, Pages 4953-4962

Molecular Characterization of Bip 1, a Monoclonal Antibody That Modulates IgE Binding to Birch Pollen Allergen, Bet v 1

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; BET V 1 PROTEINS, BETULA PENDULA; COMPLEMENTARY DNA; IMMUNOGLOBULIN E; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 0030443234     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (58)

References (52)
  • 1
    • 0024443144 scopus 로고
    • The gene coding for the major birch pollen allergen Bet v I, is highly homologous to a pea disease resistance response gene
    • Breiteneder, H., K. Pettenburger, A. Bito, R. Valenta, D. Kraft, H. Rumpold, O. Scheiner, and M. Breitenbach. 1989. The gene coding for the major birch pollen allergen Bet v I, is highly homologous to a pea disease resistance response gene. EMBO J. 8:1935.
    • (1989) EMBO J. , vol.8 , pp. 1935
    • Breiteneder, H.1    Pettenburger, K.2    Bito, A.3    Valenta, R.4    Kraft, D.5    Rumpold, H.6    Scheiner, O.7    Breitenbach, M.8
  • 4
    • 0024309396 scopus 로고
    • IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of Betula verrucosa
    • Jarolim, E., H. Rumpold, A. T. Endler, H. Ebner, M. Breitenbach, O. Scheiner, and D. Kraft. 1989. IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of Betula verrucosa. Allergy 44:385.
    • (1989) Allergy , vol.44 , pp. 385
    • Jarolim, E.1    Rumpold, H.2    Endler, A.T.3    Ebner, H.4    Breitenbach, M.5    Scheiner, O.6    Kraft, D.7
  • 12
    • 0027939421 scopus 로고
    • Isolation of an immunodominant IgE hapten from an epitope expression cDNA library: Dissection of the allergic effector reaction
    • Ball, T., S. Vrtala, W. R. Sperr, P. Valent, M. Susani, D. Kraft, and R. Valenta. 1994. Isolation of an immunodominant IgE hapten from an epitope expression cDNA library: dissection of the allergic effector reaction. J. Biol. Chem. 269: 28323.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28323
    • Ball, T.1    Vrtala, S.2    Sperr, W.R.3    Valent, P.4    Susani, M.5    Kraft, D.6    Valenta, R.7
  • 15
    • 0024431870 scopus 로고
    • Monoclonal antibodies against birch pollen allergens: Characterization by immunoblotting and use for single-step affinity purification of the major birch pollen allergen Bet v I
    • Jarolim, E., M. Tejkl, M. Rohac, G. Schlerka, O. Scheiner, D. Kraft, M. Breitenbach, and H. Rumpold. 1989. Monoclonal antibodies against birch pollen allergens: characterization by immunoblotting and use for single-step affinity purification of the major birch pollen allergen Bet v I. Int. Arch. Allergy Immunol. 90:54.
    • (1989) Int. Arch. Allergy Immunol. , vol.90 , pp. 54
    • Jarolim, E.1    Tejkl, M.2    Rohac, M.3    Schlerka, G.4    Scheiner, O.5    Kraft, D.6    Breitenbach, M.7    Rumpold, H.8
  • 16
    • 0027431127 scopus 로고
    • Properties of tree and grass pollen allergens: Reinvestigation of the linkage between solubility and allergenicity
    • Vrtala, S., M. Grote, M. Duchêne, R. van Ree, D. Kraft, O. Scheiner, and R. Valenta. 1993. Properties of tree and grass pollen allergens: reinvestigation of the linkage between solubility and allergenicity. Int. Arch. Allergy Immunol. 102: 160.
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 160
    • Vrtala, S.1    Grote, M.2    Duchêne, M.3    Van Ree, R.4    Kraft, D.5    Scheiner, O.6    Valenta, R.7
  • 18
    • 0026724030 scopus 로고
    • Diagnosis of grass pollen allergy with recombinant timothy grass (Phleum pratense) pollen allergens
    • Valenta, R., S. Vrtala, C. Ebner, D. Kraft, and O. Scheiner. 1992. Diagnosis of grass pollen allergy with recombinant timothy grass (Phleum pratense) pollen allergens. Int. Arch. Allergy Immunol. 97:287.
    • (1992) Int. Arch. Allergy Immunol. , vol.97 , pp. 287
    • Valenta, R.1    Vrtala, S.2    Ebner, C.3    Kraft, D.4    Scheiner, O.5
  • 19
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • Barbas, C. F., A. S. Kang, R. A. Lerner, and S. J. Benkovic. 1991. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. USA 88:7978.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7978
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 21
    • 44949280863 scopus 로고
    • Combinatorial immunoglobulin libraries on the surface of phage (Phabs): Rapid selection of antigen-specific Fabs
    • Barbas, C. F., III, and R. A. Lerner. 1991. Combinatorial immunoglobulin libraries on the surface of phage (Phabs): rapid selection of antigen-specific Fabs. Methods (Orlando) 2:119.
    • (1991) Methods (Orlando) , vol.2 , pp. 119
    • Barbas III, C.F.1    Lerner, R.A.2
  • 23
    • 0022539027 scopus 로고
    • Peptide and protein molecular weight determination by electrophoresis using a high molarity Tris buffer system without urea
    • Fling, S. P., and D. S. Gregerson. 1986. Peptide and protein molecular weight determination by electrophoresis using a high molarity Tris buffer system without urea. Anal. Biochem. 155:83.
    • (1986) Anal. Biochem. , vol.155 , pp. 83
    • Fling, S.P.1    Gregerson, D.S.2
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfers of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfers of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 0021760092 scopus 로고
    • A comprehensive set of analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of analysis programs for the VAX. Nucleic Acids Res. 12:387.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 27
    • 0028847256 scopus 로고
    • Molecular characterization of Api g 1, the major allergen of celery (Apium graveolens), and its immunological and structural relationships to a group of 17-kD tree pollen allergens
    • Breiteneder, H., K. Hoffmann-Sommergruber, G. O'Riordain, M. Susani, H. Ahorn, C. Ebner, D. Kraft, and O. Scheiner. 1995. Molecular characterization of Api g 1, the major allergen of celery (Apium graveolens), and its immunological and structural relationships to a group of 17-kD tree pollen allergens. Eur. J. Biochem. 233:484.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 484
    • Breiteneder, H.1    Hoffmann-Sommergruber, K.2    O'Riordain, G.3    Susani, M.4    Ahorn, H.5    Ebner, C.6    Kraft, D.7    Scheiner, O.8
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584
    • Rost, B.1    Sander, C.2
  • 30
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55.
    • (1994) Proteins , vol.19 , pp. 55
    • Rost, B.1    Sander, C.2
  • 34
    • 0019005874 scopus 로고
    • Determination of protein structure in solution by vacuum ultraviolet circular dichroism
    • Brahms, S., and J. Brahms. 1980. Determination of protein structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138:149.
    • (1980) J. Mol. Biol. , vol.138 , pp. 149
    • Brahms, S.1    Brahms, J.2
  • 35
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel beta-sheet in proteins
    • Perczel, A., K. Park, and G. D. Fasman. 1992. Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel beta-sheet in proteins. Proteins 13:57.
    • (1992) Proteins , vol.13 , pp. 57
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 36
    • 0028944711 scopus 로고
    • Domain interactions stabilize the alternatively folded state of an antibody Fab fragment
    • Lilie, H., and I. Bruchner. 1995. Domain interactions stabilize the alternatively folded state of an antibody Fab fragment. FEBS Lett. 362:43.
    • (1995) FEBS Lett. , vol.362 , pp. 43
    • Lilie, H.1    Bruchner, I.2
  • 37
    • 0029028998 scopus 로고
    • Identification of allergens in fruits and vegetables, IgE crossreactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin)
    • Ebner, C., R. Hirschwehr, L. Bauer, H. Breiteneder, R. Valenta, H. Ebner, D. Kraft, and O. Scheiner. 1995. Identification of allergens in fruits and vegetables, IgE crossreactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin). J. Allergy Clin. Immunol. 95:962.
    • (1995) J. Allergy Clin. Immunol. , vol.95 , pp. 962
    • Ebner, C.1    Hirschwehr, R.2    Bauer, L.3    Breiteneder, H.4    Valenta, R.5    Ebner, H.6    Kraft, D.7    Scheiner, O.8
  • 39
    • 0028877602 scopus 로고
    • Structural features of the reactions of antibodies and proteins
    • Braden, C. B., and R. J. Poljak. 1995. Structural features of the reactions of antibodies and proteins. FASEB J. 9:9.
    • (1995) FASEB J. , vol.9 , pp. 9
    • Braden, C.B.1    Poljak, R.J.2
  • 40
    • 0023905451 scopus 로고
    • Monoclonal antibodies as probes of conformational changes in protein-engineered cytochrome c
    • Collawn, J. F., C. J. A. Wallace, A. E. I. Proudfoot, and Y. Paterson. 1988. Monoclonal antibodies as probes of conformational changes in protein-engineered cytochrome c. J. Biol. Chem. 263:8625.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8625
    • Collawn, J.F.1    Wallace, C.J.A.2    Proudfoot, A.E.I.3    Paterson, Y.4
  • 42
    • 0024298964 scopus 로고
    • How do enzymes work?
    • Kraut, J. 1988. How do enzymes work? Science 242:533.
    • (1988) Science , vol.242 , pp. 533
    • Kraut, J.1
  • 43
    • 0025730616 scopus 로고
    • At the crossroads of chemistry and immunology: Catalytic antibodies
    • Lerner, R. A., S. J. Benkovic, and P. G. Schultz. 1991. At the crossroads of chemistry and immunology: catalytic antibodies. Science 252:659.
    • (1991) Science , vol.252 , pp. 659
    • Lerner, R.A.1    Benkovic, S.J.2    Schultz, P.G.3
  • 45
    • 0028439575 scopus 로고
    • Antibody catalyzed cationic cyclization
    • Li, T., K. D. Janda, J. A. Ashley, and R. A. Lerner. 1994. Antibody catalyzed cationic cyclization. Science 264:1289.
    • (1994) Science , vol.264 , pp. 1289
    • Li, T.1    Janda, K.D.2    Ashley, J.A.3    Lerner, R.A.4
  • 47
    • 0027489204 scopus 로고
    • Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: Production of a catalytic antibody with a cholinesterase activity
    • Izadyar, L., A. Friboulet, M. H. Remy, A. Roseto, and D. Thomas. 1993. Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity. Proc. Natl. Acad. Sci. USA 90:8876.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8876
    • Izadyar, L.1    Friboulet, A.2    Remy, M.H.3    Roseto, A.4    Thomas, D.5
  • 48
    • 0028926386 scopus 로고
    • Anti-acetylcholinesterase antibodies display cholinesterase-like activity
    • Johnson, G., and S. W. Moore. 1995. Anti-acetylcholinesterase antibodies display cholinesterase-like activity. Eur. J. Immunol. 25:25.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 25
    • Johnson, G.1    Moore, S.W.2
  • 49
    • 0028027058 scopus 로고
    • Crystal structure of a catalytic antibody with a serine prolease active site
    • Zhou, G. W., J. Guo, W. Huang, R. J. Fletterick, and T. S. Scanlan. 1994. Crystal structure of a catalytic antibody with a serine prolease active site. Science 265: 1059.
    • (1994) Science , vol.265 , pp. 1059
    • Zhou, G.W.1    Guo, J.2    Huang, W.3    Fletterick, R.J.4    Scanlan, T.S.5
  • 50
    • 0028127014 scopus 로고
    • Proteolytic activity of an antibody light chain
    • Sun, M., Q. Sheng, L. Li, and S. Paul. 1994. Proteolytic activity of an antibody light chain. J. Immunol. 153:5121.
    • (1994) J. Immunol. , vol.153 , pp. 5121
    • Sun, M.1    Sheng, Q.2    Li, L.3    Paul, S.4
  • 52
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner, J. 1996. Supervising the fold: functional principles of molecular chaperones. FASEB J. 10:10.
    • (1996) FASEB J. , vol.10 , pp. 10
    • Buchner, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.