메뉴 건너뛰기




Volumn 17, Issue 2, 1999, Pages 170-175

Mutagenesis and selection of PDZ domains that bind new protein targets

Author keywords

In vivo screening; Intracellular targeting; PDZ domains; Protein engineering

Indexed keywords

MEMBRANE PROTEIN; PROTEIN;

EID: 0032966813     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/6172     Document Type: Article
Times cited : (77)

References (36)
  • 1
    • 0030220851 scopus 로고    scopus 로고
    • Engineering new functions and altering existing functions
    • Shao, Z. and Arnold, F.H. 1996. Engineering new functions and altering existing functions. Curr. Opin. Struct. Biol. 6:513-518.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 513-518
    • Shao, Z.1    Arnold, F.H.2
  • 2
    • 0030864556 scopus 로고    scopus 로고
    • 3D structural information as a guide to protein engineering using genetic selection
    • Kast, P. and Hilvert, D. 1997. 3D structural information as a guide to protein engineering using genetic selection. Curr. Opin. Struct. Biol. 7:470-479.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 470-479
    • Kast, P.1    Hilvert, D.2
  • 3
    • 0030822252 scopus 로고    scopus 로고
    • Scaffolds for engineering novel binding sites in proteins
    • Nygren, P.A. and Uhlen, M. 1997, Scaffolds for engineering novel binding sites in proteins. Curr. Opin. Struct. Biol. 7:463-469.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 463-469
    • Nygren, P.A.1    Uhlen, M.2
  • 4
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord, K., Gunneriusson, E., Ringdahl, J., Stahl, S., Uhlen, M., and Nygren P-A. 1997. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat. Biotechnol. 15:772-777.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Stahl, S.4    Uhlen, M.5    Nygren, P.-A.6
  • 5
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-membranous sites
    • Ponting, C.P., Phillips, C., Davies, K.E., and Blake, D.J. 1997. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 19:469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 6
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J. and Heldin, C.H. 1996. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21:455-458.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 7
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang, Z., Fanning, A.S., Fu, C., Xu, J., Marfatia, S.M., Chisti, A.H. et al. 1997. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275:73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1    Fanning, A.S.2    Fu, C.3    Xu, J.4    Marfatia, S.M.5    Chisti, A.H.6
  • 8
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.C., Schenker, L.T., Kennedy, M.B., and Seeburg, P.M. 1995. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269:1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.M.4
  • 9
  • 10
    • 0030734979 scopus 로고    scopus 로고
    • PDZ domains and the formation of protein networks at the plasma membrane
    • Fanning, A.S. and Anderson, J.M. 1998. PDZ domains and the formation of protein networks at the plasma membrane. Curr. Top. Microbiol. Immunol. 228:209-233.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.228 , pp. 209-233
    • Fanning, A.S.1    Anderson, J.M.2
  • 11
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G.B., Ren, R., and Baltimore, D. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 12
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. 1995. Protein modules and signalling networks. Nature 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 13
    • 0344283030 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kurian, J. and Cowburn, D. 1997. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 16:6141-6150.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.16 , pp. 6141-6150
    • Kurian, J.1    Cowburn, D.2
  • 14
    • 0027373678 scopus 로고
    • Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation
    • Prasad, R., Gu. Y., Alder, H., Nakamura, T., Canaani, O., Saito, H. et al. 1993. Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation. Cancer Res. 53:5624-5628.
    • (1993) Cancer Res. , vol.53 , pp. 5624-5628
    • Prasad, R.1    Gu, Y.2    Alder, H.3    Nakamura, T.4    Canaani, O.5    Saito, H.6
  • 15
    • 0005693718 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R.C. and Joyce, G.F. 1992. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 26:259-288.
    • (1992) PCR Methods Appl. , vol.26 , pp. 259-288
    • Cadwell, R.C.1    Joyce, G.F.2
  • 16
    • 0027251721 scopus 로고
    • The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit
    • Durfee, T., Becherer, K., Chen, P.L., Yen, S.H., Yang, Y., Kilburn, A.E. et al. 1993. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7:555-569.
    • (1993) Genes Dev. , vol.7 , pp. 555-569
    • Durfee, T.1    Becherer, K.2    Chen, P.L.3    Yen, S.H.4    Yang, Y.5    Kilburn, A.E.6
  • 17
    • 0028998860 scopus 로고
    • Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member
    • Callahan, C.A., Muralidhar, M.G., Lundgren, S.E., Scully, A.L., and Thomas, J.B. 1995. Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member. Nature 376:171-174.
    • (1995) Nature , vol.376 , pp. 171-174
    • Callahan, C.A.1    Muralidhar, M.G.2    Lundgren, S.E.3    Scully, A.L.4    Thomas, J.B.5
  • 18
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S.J. Gale, N.W., Mbamalu, G., Yancopoulos, G.D., Henkemeyer, M., and Pawson, T. 1996. Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383:722-725.
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4    Henkemeyer, M.5    Pawson, T.6
  • 20
    • 0039793622 scopus 로고    scopus 로고
    • SAP102. A novel postsynaptic protein that interacts with NMDA receptor complexes in vivo
    • Müller, B.M., Bistner, U., Kindler, S., Chung, W.K., Kuhlendahl, S., Fenster, S.D. et al. 1996. SAP102. a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron 17:255-265.
    • (1996) Neuron , vol.17 , pp. 255-265
    • Müller, B.M.1    Bistner, U.2    Kindler, S.3    Chung, W.K.4    Kuhlendahl, S.5    Fenster, S.D.6
  • 21
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M., and McKinnon R. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85:1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    McKinnon, R.6
  • 22
    • 0031016269 scopus 로고    scopus 로고
    • Intrabodies: Turning the humoral immune system outside in for intracellular immunization
    • Marasco, W.A. 1997. Intrabodies: turning the humoral immune system outside in for intracellular immunization. Gene. Ther. 4:11-15.
    • (1997) Gene. Ther. , vol.4 , pp. 11-15
    • Marasco, W.A.1
  • 23
    • 0031566160 scopus 로고    scopus 로고
    • Characterization of scFv-421, a single-chain antibody targeted to p53
    • Jannot, C.B. and Hynes, N.E. 1997. Characterization of scFv-421, a single-chain antibody targeted to p53. Biochem. Biophys. Res. Commun. 230:242-246.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 242-246
    • Jannot, C.B.1    Hynes, N.E.2
  • 24
    • 0028223378 scopus 로고
    • In vitro selection from protein and peptide libraries
    • Clackson, T. and Wells, J.A. 1994. In vitro selection from protein and peptide libraries. Trends Biotechnol. 12:173-184.
    • (1994) Trends Biotechnol. , vol.12 , pp. 173-184
    • Clackson, T.1    Wells, J.A.2
  • 25
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade
    • Tsunoda, S., Sierralta, J., Sun, Y., Bodner, R., Suzuki, E., Becker, A. et al. 1997. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. Nature 388:243-249.
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Becker, A.6
  • 26
    • 0021827802 scopus 로고
    • Transformation of yeast with linearized plasmid DNA. Formation of inverted dimers and recombinant plasmid products
    • Kunes, S., Botstein, D., and Fox, M.S. 1985. Transformation of yeast with linearized plasmid DNA. Formation of inverted dimers and recombinant plasmid products. J. Mol. Biol. 184:375-387.
    • (1985) J. Mol. Biol. , vol.184 , pp. 375-387
    • Kunes, S.1    Botstein, D.2    Fox, M.S.3
  • 27
    • 0028854837 scopus 로고
    • A B-cell coactivator of octamer-binding transcription factors
    • Gstaiger, M., Knoepfel, L., Georgiev, O., Schaffner, W., and Hovens, C.M. 1995. A B-cell coactivator of octamer-binding transcription factors. Nature 373:360-362.
    • (1995) Nature , vol.373 , pp. 360-362
    • Gstaiger, M.1    Knoepfel, L.2    Georgiev, O.3    Schaffner, W.4    Hovens, C.M.5
  • 28
    • 0029882332 scopus 로고    scopus 로고
    • An in vitro assay of betagalactosidase from yeast
    • Schneider, S., Buchert, M., and Hovens, C.M. 1996. An in vitro assay of betagalactosidase from yeast. Biotechniques 20:960-962.
    • (1996) Biotechniques , vol.20 , pp. 960-962
    • Schneider, S.1    Buchert, M.2    Hovens, C.M.3
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 31
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Paterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 32
    • 0030767578 scopus 로고    scopus 로고
    • An epitope tagged mammalian/ prokaryotic expression vector with positive selection of cloned inserts
    • Schneider, S., Georgiev, O., Buchert, M., Adams, M.T., Moelling, K., and Hovens, C.M. 1997. An epitope tagged mammalian/ prokaryotic expression vector with positive selection of cloned inserts. Gene 197:337-341.
    • (1997) Gene , vol.197 , pp. 337-341
    • Schneider, S.1    Georgiev, O.2    Buchert, M.3    Adams, M.T.4    Moelling, K.5    Hovens, C.M.6
  • 33
    • 0030994417 scopus 로고    scopus 로고
    • Identification of XLerk, an Eph family ligand regulated during mesoderm induction and neurogenesis in Xenopus laevis
    • Jones, T.L., Karavanova, I., Chong, L., Zhou, R.P., and Daar, I.O. 1997. Identification of XLerk, an Eph family ligand regulated during mesoderm induction and neurogenesis in Xenopus laevis. Oncogene 14:2159-2166.
    • (1997) Oncogene , vol.14 , pp. 2159-2166
    • Jones, T.L.1    Karavanova, I.2    Chong, L.3    Zhou, R.P.4    Daar, I.O.5
  • 34
    • 0028793176 scopus 로고
    • Methods for sites controlled coupling to carboxymethylated dextran surfaces in surface plasmon resonance sensors
    • Lofas, S., Johnsson, B., Edstrom, A., Hansson, A., Lindquist, G., Muller, R.M., and Stigh, L. 1995. Methods for sites controlled coupling to carboxymethylated dextran surfaces in surface plasmon resonance sensors. Biosens. Bioelect. 10:813-822.
    • (1995) Biosens. Bioelect. , vol.10 , pp. 813-822
    • Lofas, S.1    Johnsson, B.2    Edstrom, A.3    Hansson, A.4    Lindquist, G.5    Muller, R.M.6    Stigh, L.7
  • 35
    • 0030738902 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor. A comparison of immobilisation strategies
    • Catimel, B., Nerrie, M., Lee, F.T., Scott, A.M., Ritter, G., Welt, S. et al. 1997. Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor. A comparison of immobilisation strategies. J. Chromatogr. A. 776:15-30.
    • (1997) J. Chromatogr. A. , vol.776 , pp. 15-30
    • Catimel, B.1    Nerrie, M.2    Lee, F.T.3    Scott, A.M.4    Ritter, G.5    Welt, S.6
  • 36
    • 0029053412 scopus 로고
    • Interpreting complex binding kinetics from optical biosensors: A comparison of analysis by linearization, the integrated rate equation, and numerical integration
    • Morten, T.A., Myszka, D.G., and Chalken, I.M. 1995. Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the integrated rate equation, and numerical integration. Anal. Biochem. 227:176-185.
    • (1995) Anal. Biochem. , vol.227 , pp. 176-185
    • Morten, T.A.1    Myszka, D.G.2    Chalken, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.