메뉴 건너뛰기




Volumn 12, Issue 11, 2003, Pages 2549-2558

Modulating the binding properties of an anti-17β-estradiol antibody by systematic mutation combinations

Author keywords

Antibody; Estradiol; Mutation; Site directed mutagenesis; Steroid

Indexed keywords

ESTRADIOL ANTIBODY; ESTRONE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; TESTOSTERONE;

EID: 0142179040     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0353903     Document Type: Article
Times cited : (23)

References (22)
  • 1
    • 0025838021 scopus 로고    scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces. The gene III site
    • Barbas III, C.F., Kang, A.S., Lerner, R.A., and Benkovic, S.J. Assembly of combinatorial antibody libraries on phage surfaces. The gene III site. Proc. Natl. Acad. Sci. 88: 7978-7982.
    • Proc. Natl. Acad. Sci. , vol.88 , pp. 7978-7982
    • Barbas C.F. III1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 2
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter, P.J., Winter, G., Wilkinson, A.J., and Fersht, A.R. 1984. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38: 835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 3
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A.E., Baase, W.A., Zhang, X.J., Heinz, D.W., Blaber, M., Baldwin, E.P., and Matthews, B.W. 1992. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255: 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 4
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote, J. and Winter, G. 1992. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224: 487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 5
    • 0027768856 scopus 로고
    • The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen: The interaction of mutant D1.3 antibodies with lysozyme
    • Hawkins, R.E., Russell, S.J., Baier, M., and Winter, G. 1993. The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen: The interaction of mutant D1.3 antibodies with lysozyme. J. Mol. Biol. 234: 958-964.
    • (1993) J. Mol. Biol. , vol.234 , pp. 958-964
    • Hawkins, R.E.1    Russell, S.J.2    Baier, M.3    Winter, G.4
  • 6
    • 0023645205 scopus 로고
    • Non-additivity in protein-protein interactions
    • Horovitz, A. 1987. Non-additivity in protein-protein interactions. J. Mol. Biol. 196: 733-735.
    • (1987) J. Mol. Biol. , vol.196 , pp. 733-735
    • Horovitz, A.1
  • 7
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • Horovitz, A., and Fersht, A.R. 1990. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214: 613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 8
    • 0035965352 scopus 로고    scopus 로고
    • Crystal structure of a recombinant anti-estradiol Fab fragment in complex with 17β-estradiol
    • Lamminmaki, U. and Kankare, J.A. 2001. Crystal structure of a recombinant anti-estradiol Fab fragment in complex with 17β-estradiol. J. Biol. Chem. 276: 36687-36694.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36687-36694
    • Lamminmaki, U.1    Kankare, J.A.2
  • 11
    • 0035253598 scopus 로고    scopus 로고
    • The integrity of the ball-and-socket joint between V and C domains is essential for complete activity of a humanized antibody
    • Landolfi, N.F., Thakur, A.B., Fu, H., Vasquez, M., Queen, C., and Tsurushita, N. 2001. The integrity of the ball-and-socket joint between V and C domains is essential for complete activity of a humanized antibody. J. Immunol. 166: 1748-1754.
    • (2001) J. Immunol. , vol.166 , pp. 1748-1754
    • Landolfi, N.F.1    Thakur, A.B.2    Fu, H.3    Vasquez, M.4    Queen, C.5    Tsurushita, N.6
  • 12
    • 0023710629 scopus 로고
    • Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint
    • Lesk, A.M. and Chothia, C. 1988. Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint. Nature 335: 188-190.
    • (1988) Nature , vol.335 , pp. 188-190
    • Lesk, A.M.1    Chothia, C.2
  • 13
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews, B.W. 1995. Studies on protein stability with T4 lysozyme. Adv. Protein Chem. 46: 249-278.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 14
    • 0033136580 scopus 로고    scopus 로고
    • Synthesis of novel europium-labeled estradiol derivatives for time-resolved fluoroimmunoassays
    • Meltola, N., Jauria, P., Saviranta, P., and Mikola, H. 1999. Synthesis of novel europium-labeled estradiol derivatives for time-resolved fluoroimmunoassays. Bioconjug. Chem. 10: 325-331.
    • (1999) Bioconjug. Chem. , vol.10 , pp. 325-331
    • Meltola, N.1    Jauria, P.2    Saviranta, P.3    Mikola, H.4
  • 15
    • 0027194733 scopus 로고
    • Labeling of estradiol and testosterone alkyloxime derivatives with a europium chelate for time-resolved fluoroimmunoassays
    • Mikola, H., Sundell, A.C., and Hanninen, E. 1993. Labeling of estradiol and testosterone alkyloxime derivatives with a europium chelate for time-resolved fluoroimmunoassays. Steroids 58: 330-334.
    • (1993) Steroids , vol.58 , pp. 330-334
    • Mikola, H.1    Sundell, A.C.2    Hanninen, E.3
  • 16
    • 0024587787 scopus 로고
    • The synthesis and use of activated N-benzyl derivatives of diethylenetriaminetetraacetic acids: Alternative reagents for labeling of antibodies with metal ions
    • Mukkala, V.M., Mikola, H., and Hemmila, I. 1989. The synthesis and use of activated N-benzyl derivatives of diethylenetriaminetetraacetic acids: Alternative reagents for labeling of antibodies with metal ions. Anal. Biochem. 176: 319-325.
    • (1989) Anal. Biochem. , vol.176 , pp. 319-325
    • Mukkala, V.M.1    Mikola, H.2    Hemmila, I.3
  • 19
    • 85081432583 scopus 로고    scopus 로고
    • Immunoassay improvement by molecular engineering
    • Turku University, Turku, Finland
    • Saviranta, P. 2001. Immunoassay improvement by molecular engineering. In Annales Universitatis Turkuensis (series). Turku University, Turku, Finland.
    • (2001) Annales Universitatis Turkuensis (Series)
    • Saviranta, P.1
  • 20
    • 0031917485 scopus 로고    scopus 로고
    • Engineering the steroid-specificity of an anti-17β-estradiol Fab by random mutagenesis and competitive phage panning
    • Saviranta, P., Pajunen, M., Jauria, P., Karp, M., Pettersson, K., Mantsala, P., and Lovgren, T. 1998. Engineering the steroid-specificity of an anti-17β-estradiol Fab by random mutagenesis and competitive phage panning. Protein Eng. 11: 143-152.
    • (1998) Protein Eng. , vol.11 , pp. 143-152
    • Saviranta, P.1    Pajunen, M.2    Jauria, P.3    Karp, M.4    Pettersson, K.5    Mantsala, P.6    Lovgren, T.7
  • 21
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J.A. 1990. Additivity of mutational effects in proteins. Biochemistry 29: 8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 22
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu, J., Baase, W.A., Baldwin, E., and Matthews, B.W. 1998. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7: 158-177.
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.