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Volumn 15, Issue 3, 1999, Pages 391-396

Constrained cell recognition peptides engineered into streptavidin

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE SYNTHESIS; PROTEIN ENGINEERING; STREPTAVIDIN;

EID: 0033136108     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp990043n     Document Type: Article
Times cited : (21)

References (21)
  • 1
    • 0025787973 scopus 로고
    • A streptavidin-protein A chimera that allows one-step production of a variety of specific antibody conjugates
    • Sano, T.; Cantor, C. R. A streptavidin-protein A chimera that allows one-step production of a variety of specific antibody conjugates. Bio/Technology 1991, 9, 1378-1381.
    • (1991) Bio/Technology , vol.9 , pp. 1378-1381
    • Sano, T.1    Cantor, C.R.2
  • 2
    • 0026601975 scopus 로고
    • A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions
    • Sano, T.; Glazer, A. N.; Cantor, C. R. A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 1534-1538.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1534-1538
    • Sano, T.1    Glazer, A.N.2    Cantor, C.R.3
  • 3
    • 0028889940 scopus 로고
    • Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv)
    • Dubel, S.; Breitling, F.; Kontermann, R.; Schmidt, T.; Skerra, A.; Little, M. Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv). J. Immunol. Methods 1995, 178, 201-209.
    • (1995) J. Immunol. Methods , vol.178 , pp. 201-209
    • Dubel, S.1    Breitling, F.2    Kontermann, R.3    Schmidt, T.4    Skerra, A.5    Little, M.6
  • 4
    • 0029878864 scopus 로고    scopus 로고
    • Identification of biotinylated molecules using a baculovirus-expressed luciferase-streptavidin fusion protein
    • Karp, M.; Lindqvist, C.; Nissinen, R.; Wahlbeck, S.; Akerman, K.; Oker-Blom, C. Identification of biotinylated molecules using a baculovirus-expressed luciferase-streptavidin fusion protein. Biotechniques 1996, 20, 452-459.
    • (1996) Biotechniques , vol.20 , pp. 452-459
    • Karp, M.1    Lindqvist, C.2    Nissinen, R.3    Wahlbeck, S.4    Akerman, K.5    Oker-Blom, C.6
  • 5
    • 0030575193 scopus 로고    scopus 로고
    • Highly efficient production of gfp and its derivatives in insect cells for visual in vitro applications
    • Oker-Blom, C.; Orellana, A.; Keinanen, K. Highly efficient production of GFP and its derivatives in insect cells for visual in vitro applications. FEBS Lett. 1996, 389, 238-243.
    • (1996) FEBS Lett. , vol.389 , pp. 238-243
    • Oker-Blom, C.1    Orellana, A.2    Keinanen, K.3
  • 7
    • 0026460183 scopus 로고
    • Engineering of artificial cell adhesion proteins by grafting the Arg-Gly-Asp cell adhesive signal to a calpastatin segment
    • Hashino, K.; Shimojo, T.; Kimizuka, F.; Kato, I.; Maeda, T.; Sekiguchi, K.; Titani, K. Engineering of artificial cell adhesion proteins by grafting the Arg-Gly-Asp cell adhesive signal to a calpastatin segment. J. Biochem. 1992, 112, 547-551.
    • (1992) J. Biochem. , vol.112 , pp. 547-551
    • Hashino, K.1    Shimojo, T.2    Kimizuka, F.3    Kato, I.4    Maeda, T.5    Sekiguchi, K.6    Titani, K.7
  • 8
    • 0027433096 scopus 로고
    • High-affinity self-reactive human antibodies by design and selection: Targeting the integrin ligand binding site
    • Barbas, C. F., III; Languino, L. R.; Smith, J. W. High-affinity self-reactive human antibodies by design and selection: Targeting the integrin ligand binding site. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 10003-10007.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10003-10007
    • Barbas C.F. III1    Languino, L.R.2    Smith, J.W.3
  • 9
    • 0028927072 scopus 로고
    • Engineered idiotypes. Immunochemical analysis of antigenized antibodies expressing a conformationally constrained Arg-Gly-Asp motif
    • Rossi, F.; Billeta, R.; Ruggeri, Z.; Zanetti, M. Engineered idiotypes. Immunochemical analysis of antigenized antibodies expressing a conformationally constrained Arg-Gly-Asp motif. Mol. Immunol. 1995, 32, 341-346.
    • (1995) Mol. Immunol. , vol.32 , pp. 341-346
    • Rossi, F.1    Billeta, R.2    Ruggeri, Z.3    Zanetti, M.4
  • 11
    • 0028947622 scopus 로고
    • Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme
    • Yamada, T.; Song, H.; Inaka, K.; Shimada, Y.; Kikuchi, M.; Matsushima, M. Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme. J. Biol. Chem. 1995, 270, 5687-5690.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5687-5690
    • Yamada, T.1    Song, H.2    Inaka, K.3    Shimada, Y.4    Kikuchi, M.5    Matsushima, M.6
  • 12
    • 0028910003 scopus 로고
    • Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: Contributions of tryptophan residues 79, 108, and 120
    • Chilkoti, A.; Tan P. H.; Stayton, P. S. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: Contributions of tryptophan residues 79, 108, and 120. Proc. Natl. Acad. Sci U.S.A. 1995, 92, 1754-1758.
    • (1995) Proc. Natl. Acad. Sci U.S.A. , vol.92 , pp. 1754-1758
    • Chilkoti, A.1    Tan, P.H.2    Stayton, P.S.3
  • 13
    • 0032568575 scopus 로고    scopus 로고
    • Energetic roles of hydrogen bonds at the ureido oxygen binding pocket in the streptavidin-biotin complex
    • Klumb, L. A.; Chu, V.; Stayton, P. S. Energetic roles of hydrogen bonds at the ureido oxygen binding pocket in the streptavidin-biotin complex. Biochemistry 1998, 37, 657-7663.
    • (1998) Biochemistry , vol.37 , pp. 657-7663
    • Klumb, L.A.1    Chu, V.2    Stayton, P.S.3
  • 14
    • 0028118893 scopus 로고
    • Osteopontin promotes vascular cell adhesion and spreading and is chemotactic for smooth muscle cells in vitro
    • Liaw, L.; Almeida M.; Hart, C. E.; Schwartz, S. M.; Giachelli, C. M. Osteopontin promotes vascular cell adhesion and spreading and is chemotactic for smooth muscle cells in vitro. Circ. Res. 1994, 74, 214-224.
    • (1994) Circ. Res. , vol.74 , pp. 214-224
    • Liaw, L.1    Almeida, M.2    Hart, C.E.3    Schwartz, S.M.4    Giachelli, C.M.5
  • 15
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A. L.; Harvey, T. S.; Baron, M.; Boyd, J.; Campbell, I. D. The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions. Cell 1992, 71, 671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 16
    • 0023609864 scopus 로고
    • Influence of stereo-chemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher, M. D.; Ruoslahti, E. Influence of stereo-chemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol Chem. 1987, 262, 17294-17298.
    • (1987) J. Biol Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 17
    • 0025866591 scopus 로고
    • Artificial cell adhesive proteins engineered by grafting the Arg-Gly-Asp cell recognition signal: Factors modulating the cell adhesive activity of the grafted signal
    • Maeda, T.; Hashino, K.; Oyama, R.; Titani, K.; Sekiguchi, K. Artificial cell adhesive proteins engineered by grafting the Arg-Gly-Asp cell recognition signal: Factors modulating the cell adhesive activity of the grafted signal. J. Biochem. 1991, 110, 381-387.
    • (1991) J. Biochem. , vol.110 , pp. 381-387
    • Maeda, T.1    Hashino, K.2    Oyama, R.3    Titani, K.4    Sekiguchi, K.5
  • 18
    • 0025814801 scopus 로고
    • Arginyl-glycyl-aspartic acid (RGD): A cell adhesion motif
    • D'Souza, S. E.; Ginsberg, M. H.; Plow, E. F. Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends Biochem. Sci. 1981, 16, 246-250.
    • (1981) Trends Biochem. Sci. , vol.16 , pp. 246-250
    • D'Souza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 19
    • 0025113791 scopus 로고
    • Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin
    • Alon, R.; Bayer, E. A.; Wilchek, M. Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin. Biochem. Biophys. Res. Commun. 1990, 170, 1236-1241.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1236-1241
    • Alon, R.1    Bayer, E.A.2    Wilchek, M.3
  • 20
    • 0026910431 scopus 로고
    • Cell-adhesive properties of streptavidin are mediated by the exposure of an RGD-like RYD site
    • Alon, R.; Bayer, E. A.; Wilchek, M. Cell-adhesive properties of streptavidin are mediated by the exposure of an RGD-like RYD site. Eur. J. Cell Biol. 1992, 58, 271-279.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 271-279
    • Alon, R.1    Bayer, E.A.2    Wilchek, M.3
  • 21
    • 0027416003 scopus 로고
    • Streptavidin blocks immune reactions mediated by fibronectin-VLA-5 recognition through an Arg-Gly-Asp mimicking site
    • Alon, R.; Hershkoviz, R.; Bayer, E. A.; Wilchek, M.; Lider, O. Streptavidin blocks immune reactions mediated by fibronectin-VLA-5 recognition through an Arg-Gly-Asp mimicking site. Eur. J. Immunol. 1993, 23, 893-898.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 893-898
    • Alon, R.1    Hershkoviz, R.2    Bayer, E.A.3    Wilchek, M.4    Lider, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.