메뉴 건너뛰기




Volumn 230, Issue 1-2, 1999, Pages 121-130

Fluobodies: Green fluorescent single-chain Fv fusion proteins

Author keywords

Fusion proteins; Green fluorescent protein; Single chain Fv fragments

Indexed keywords

FLUORESCEIN ISOTHIOCYANATE; FLUORESCENT DYE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LIPOPOLYSACCHARIDE; RECOMBINANT ANTIBODY;

EID: 0032758727     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(99)00131-3     Document Type: Article
Times cited : (49)

References (33)
  • 1
    • 0029761781 scopus 로고    scopus 로고
    • Simultaneous fluorescence-activated cell sorter analysis of two distinct transcriptional elements within a single cell using engineered green fluorescent proteins
    • Anderson M.T., Tjioe I.M., Lorincz M.C., Parks D.R., Herzenberg L.A., Nolan G.P. Simultaneous fluorescence-activated cell sorter analysis of two distinct transcriptional elements within a single cell using engineered green fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 93:1996;8508-8511.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8508-8511
    • Anderson, M.T.1    Tjioe, I.M.2    Lorincz, M.C.3    Parks, D.R.4    Herzenberg, L.A.5    Nolan, G.P.6
  • 2
    • 0029877190 scopus 로고    scopus 로고
    • Construction of a fusion protein between protein A and green fluorescent protein and its application to western blotting
    • Aoki T., Takahashi Y., Koch K.S., Leffert H.L., Watabe H. Construction of a fusion protein between protein A and green fluorescent protein and its application to western blotting. FEBS Lett. 384:1996;193-197.
    • (1996) FEBS Lett. , vol.384 , pp. 193-197
    • Aoki, T.1    Takahashi, Y.2    Koch, K.S.3    Leffert, H.L.4    Watabe, H.5
  • 3
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., Prasher D.C. Green fluorescent protein as a marker for gene expression. Science. 363:1994;802-805.
    • (1994) Science , vol.363 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 4
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack B.P., Valdivia R., Falkow S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 173:1996;33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.2    Falkow, S.3
  • 5
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A., Whitehorn E.A., Tate E., Stemmer W.P.C. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14:1996;315-319.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 7
    • 0031822626 scopus 로고    scopus 로고
    • Selection of Ralstonia solanacearum race 3 specific monoclonal antibodies from combinatorial libraries
    • Griep R.A., Van Twisk C., Van der Wolf J.M., Van Beckhoven J.R.C.M., Schots A. Selection of Ralstonia solanacearum race 3 specific monoclonal antibodies from combinatorial libraries. Phytopathology. 88:1998;795-803.
    • (1998) Phytopathology , vol.88 , pp. 795-803
    • Griep, R.A.1    Van Twisk, C.2    Van Der Wolf, J.M.3    Van Beckhoven, J.R.C.M.4    Schots, A.5
  • 10
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim R., Tsien R.Y. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6:1996;178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 11
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom H.R., Griffiths A.D., Johnson K.S., Chiswell D.J., Hudson P., Winter G. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 15:1991;4133-4137.
    • (1991) Nucleic Acids Res. , vol.15 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 12
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., Pease L.R. Engineering hybrid genes without the use of restriction enzymes. Gene. 77:1989;61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 14
    • 0028777967 scopus 로고
    • Expression of the gene and fluorescence characteristics of the recombinant protein
    • Inouye S., Tsuji F.I. Expression of the gene and fluorescence characteristics of the recombinant protein. FEBS Lett. 341:1994;277-280.
    • (1994) FEBS Lett. , vol.341 , pp. 277-280
    • Inouye, S.1    Tsuji, F.I.2
  • 15
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing
    • Johnson B.H., Hecht M.H. Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Bio/Technology. 12:1994;1357-1360.
    • (1994) Bio/Technology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 17
    • 0023410604 scopus 로고
    • Characterization of the Erwinia carotovora pelB gene and its product pectate lyase
    • Lei S., Lin H., Wang S., Callaway J., Wilcox G. Characterization of the Erwinia carotovora pelB gene and its product pectate lyase. J. Bacteriol. 169:1987;4379-4383.
    • (1987) J. Bacteriol. , vol.169 , pp. 4379-4383
    • Lei, S.1    Lin, H.2    Wang, S.3    Callaway, J.4    Wilcox, G.5
  • 19
    • 0023052239 scopus 로고
    • An Hsp-70 like protein in the ER: Identity with the 78 kD glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro S., Pelham H.R.B. An Hsp-70 like protein in the ER: identity with the 78 kD glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 46:1986;291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 20
    • 0028850321 scopus 로고
    • Quantitative imaging of green fluorescent protein in cultured cells: Comparison of microscopic techniques, use in fusion proteins and detection limits
    • Niswender K.D., Blackman S.M., Rohde L., Magnuson M.A., Piston D.W. Quantitative imaging of green fluorescent protein in cultured cells: comparison of microscopic techniques, use in fusion proteins and detection limits. J. Microbiol. 180:1995;109-116.
    • (1995) J. Microbiol. , vol.180 , pp. 109-116
    • Niswender, K.D.1    Blackman, S.M.2    Rohde, L.3    Magnuson, M.A.4    Piston, D.W.5
  • 21
    • 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. 389:1996;238-243.
    • (1996) FEBS Lett. , vol.389 , pp. 238-243
    • Oker-Blom, C.1    Orellana, A.2    Keinanen, K.3
  • 22
    • 1542698957 scopus 로고
    • Cloning immunoglobulin variable domains for the expression by the polymerase chain reaction
    • Orlandi O., Gussow D.H., Jones P.T., Winter G. Cloning immunoglobulin variable domains for the expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. U.S.A. 86:1989;3833-3837.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 3833-3837
    • Orlandi, O.1    Gussow, D.H.2    Jones, P.T.3    Winter, G.4
  • 25
    • 0028035693 scopus 로고
    • Microscopical studies of the infection of gerbera flowers by Botrytis cinerea
    • Salinas J., Schots A. Microscopical studies of the infection of gerbera flowers by Botrytis cinerea. Phytopathology. 84:1994;351-356.
    • (1994) Phytopathology , vol.84 , pp. 351-356
    • Salinas, J.1    Schots, A.2
  • 26
    • 0013553762 scopus 로고
    • Cloning of the immunological repertoire in Escherichia coli for generation of monoclonal catalytic antibodies, Construction of a heavy chain variable region-specific cDNA library
    • Sastry L., Alting-Mees M., Huse W.D., Short J.M., Sorge J.A., Hay B.H., Janda K.D., Benkovic S.J., Lerner R.A. Cloning of the immunological repertoire in Escherichia coli for generation of monoclonal catalytic antibodies, Construction of a heavy chain variable region-specific cDNA library. Proc. Natl. Acad. Sci. U.S.A. 86:1989;5728-5732.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5728-5732
    • Sastry, L.1    Alting-Mees, M.2    Huse, W.D.3    Short, J.M.4    Sorge, J.A.5    Hay, B.H.6    Janda, K.D.7    Benkovic, S.J.8    Lerner, R.A.9
  • 27
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0030842771 scopus 로고    scopus 로고
    • Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli
    • Tudyka T., Skerra A. Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6:1997;2180-2187.
    • (1997) Protein Sci. , vol.6 , pp. 2180-2187
    • Tudyka, T.1    Skerra, A.2
  • 29
    • 0343726593 scopus 로고
    • Serological characterization of fluorescent Pseudomonas strains cross-reacting with antibodies against Erwinia chrysanthemi
    • Van der Wolf J.M., Van Beckhoven J.R.C.M., De Boef E., Roozen N.J.M. Serological characterization of fluorescent Pseudomonas strains cross-reacting with antibodies against Erwinia chrysanthemi. Neth. J. Plant Pathol. 99:1993;51-60.
    • (1993) Neth. J. Plant Pathol. , vol.99 , pp. 51-60
    • Van Der Wolf, J.M.1    Van Beckhoven, J.R.C.M.2    De Boef, E.3    Roozen, N.J.M.4
  • 31
    • 0028227833 scopus 로고
    • Implications for bcd mRNA localization from spatial distribution of exu protein in Drosophila oogenesis
    • Wang S., Hazelrigg T. Implications for bcd mRNA localization from spatial distribution of exu protein in Drosophila oogenesis. Nature. 369:1994;400-403.
    • (1994) Nature , vol.369 , pp. 400-403
    • Wang, S.1    Hazelrigg, T.2
  • 32
    • 84985493765 scopus 로고
    • Spectral perturbations of the Aequoria green fluorescent protein
    • Ward W.W., Cody C.W., Hart R.C., Cormier M.J. Spectral perturbations of the Aequoria green fluorescent protein. Photochem. Photobiol. 31:1980;611-615.
    • (1980) Photochem. Photobiol. , vol.31 , pp. 611-615
    • Ward, W.W.1    Cody, C.W.2    Hart, R.C.3    Cormier, M.J.4
  • 33
    • 0030010676 scopus 로고    scopus 로고
    • Dual color microscopic imagery of cells expressing the green fluorescent protein and a red-shifted variant
    • Yang T.T., Kain S.R., Kitts P., Kondepudi A., Yang M.M., Youvan D.C. Dual color microscopic imagery of cells expressing the green fluorescent protein and a red-shifted variant. Gene. 173:1996;19-23.
    • (1996) Gene , vol.173 , pp. 19-23
    • Yang, T.T.1    Kain, S.R.2    Kitts, P.3    Kondepudi, A.4    Yang, M.M.5    Youvan, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.