메뉴 건너뛰기




Volumn 103, Issue 2, 2007, Pages 155-160

Effective selection system for experimental evolution of random polypeptides towards DNA-binding protein

Author keywords

artificial evolution; artificial protein; DNA binding; phage display

Indexed keywords

AMINO ACIDS; CLONING; DNA; ENZYME KINETICS; MUTAGENESIS; PROTEINS;

EID: 33947158650     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.103.155     Document Type: Article
Times cited : (2)

References (20)
  • 1
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe A.D., and Szostak J.W. Functional proteins from a random-sequence library. Nature 410 (2001) 715-718
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 3
    • 0037308696 scopus 로고    scopus 로고
    • Can an arbitrary sequence evolve towards acquiring a biological function?
    • Hayashi Y., Sakata H., Makino Y., Urabe I., and Yomo T. Can an arbitrary sequence evolve towards acquiring a biological function?. J. Mol. Evol. 56 (2003) 162-168
    • (2003) J. Mol. Evol. , vol.56 , pp. 162-168
    • Hayashi, Y.1    Sakata, H.2    Makino, Y.3    Urabe, I.4    Yomo, T.5
  • 4
    • 0842290926 scopus 로고    scopus 로고
    • Evolution of an arbitrary sequence in solubility
    • Ito Y., Kawama T., Urabe I., and Yomo T. Evolution of an arbitrary sequence in solubility. J. Mol. Evol. 58 (2003) 196-202
    • (2003) J. Mol. Evol. , vol.58 , pp. 196-202
    • Ito, Y.1    Kawama, T.2    Urabe, I.3    Yomo, T.4
  • 7
    • 0031160185 scopus 로고    scopus 로고
    • Selectively infective phage (SIP) technology: a novel method for in vivo selection of interacting protein-ligand pairs
    • Spada S., and Plückthun A. Selectively infective phage (SIP) technology: a novel method for in vivo selection of interacting protein-ligand pairs. Nat. Med. 3 (1997) 694-696
    • (1997) Nat. Med. , vol.3 , pp. 694-696
    • Spada, S.1    Plückthun, A.2
  • 8
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen P., and Winter G. Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des. 3 (1998) 321-328
    • (1998) Fold. Des. , vol.3 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 10
    • 0027994717 scopus 로고
    • Toward a code for the interactions of zinc fingers with DNA: selecting of randomized fingers displayed on phage
    • Choo Y., and Klug A. Toward a code for the interactions of zinc fingers with DNA: selecting of randomized fingers displayed on phage. Proc. Natl. Acad. Sci. USA 91 (1994) 11163-11167
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11163-11167
    • Choo, Y.1    Klug, A.2
  • 11
    • 33947117195 scopus 로고
    • Building zinc fingers by selection: toward a therapeutic application
    • Wu H., Yang W.P., and Barbas C.F. Building zinc fingers by selection: toward a therapeutic application. Proc. Natl. Acad. Sci. USA 89 (1992) 4457-4461
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4457-4461
    • Wu, H.1    Yang, W.P.2    Barbas, C.F.3
  • 13
    • 0031592941 scopus 로고    scopus 로고
    • Promotor-specific activation of gene expression directed by bacteriophage-selected zinc fingers
    • Choo Y., Castellanos A., Garcia-Hernandez B., Sanchez-Garcia I., and Klug A. Promotor-specific activation of gene expression directed by bacteriophage-selected zinc fingers. J. Mol. Biol. 273 (1997) 525-532
    • (1997) J. Mol. Biol. , vol.273 , pp. 525-532
    • Choo, Y.1    Castellanos, A.2    Garcia-Hernandez, B.3    Sanchez-Garcia, I.4    Klug, A.5
  • 15
    • 0030606499 scopus 로고    scopus 로고
    • Application of N-terminally truncated DNA polymerase from Thermus thermophilus (ΔTth polymerase) to DNA sequencing and polymerase chain reactions: comparative study of ΔTth and wild-type Tth polymerases
    • Arakawa T., Jongsareejit B., Tatsumi Y., Tanaka K., Ikeda K., Komatsubara H., Inoue H., Kawakami B., Oka M., Emi S., Yomo T., Shima Y., Negoro S., and Urabe I. Application of N-terminally truncated DNA polymerase from Thermus thermophilus (ΔTth polymerase) to DNA sequencing and polymerase chain reactions: comparative study of ΔTth and wild-type Tth polymerases. DNA Res. 3 (1996) 87-92
    • (1996) DNA Res. , vol.3 , pp. 87-92
    • Arakawa, T.1    Jongsareejit, B.2    Tatsumi, Y.3    Tanaka, K.4    Ikeda, K.5    Komatsubara, H.6    Inoue, H.7    Kawakami, B.8    Oka, M.9    Emi, S.10    Yomo, T.11    Shima, Y.12    Negoro, S.13    Urabe, I.14
  • 16
    • 0032578492 scopus 로고    scopus 로고
    • Artificial nine zinc-finger peptide with 30 base pair binding sites
    • Kamiuchi T., Abe E., Imanishi M., Kaji T., Nagaoka M., and Sugiura Y. Artificial nine zinc-finger peptide with 30 base pair binding sites. Biochemistry 37 (1998) 13827-13834
    • (1998) Biochemistry , vol.37 , pp. 13827-13834
    • Kamiuchi, T.1    Abe, E.2    Imanishi, M.3    Kaji, T.4    Nagaoka, M.5    Sugiura, Y.6
  • 17
    • 0028046895 scopus 로고
    • Selection of DNA binding sites for zinc fingers using rationally randomized DNA reveals coded interactions
    • Choo Y., and Klug A. Selection of DNA binding sites for zinc fingers using rationally randomized DNA reveals coded interactions. Proc. Natl. Acad. Sci. USA 91 (1994) 11168-11172
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11168-11172
    • Choo, Y.1    Klug, A.2
  • 18
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimmer of uninterrupted alpha helices: crystal structure of the protein-DNA complex
    • Ellenberger T.D., Brandl C.T., Struhl K., and Harrison S.C. The GCN4 basic region leucine zipper binds DNA as a dimmer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell 71 (1992) 1223-1237
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.D.1    Brandl, C.T.2    Struhl, K.3    Harrison, S.C.4
  • 19
    • 0034847620 scopus 로고    scopus 로고
    • Effects of amino acid substitution on the physicochemical properties of artificial proteins with random sequences
    • Tokuriki N., Sakamoto K., Waluyo D., Makino Y., Ogasawara K., Yutani K., Urabe I., and Yomo T. Effects of amino acid substitution on the physicochemical properties of artificial proteins with random sequences. J. Biosci. Bioeng. 92 (2001) 167-172
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 167-172
    • Tokuriki, N.1    Sakamoto, K.2    Waluyo, D.3    Makino, Y.4    Ogasawara, K.5    Yutani, K.6    Urabe, I.7    Yomo, T.8
  • 20
    • 0000484499 scopus 로고
    • Hydrophobic parameter π of amino-acid side chains from the partitioning of N-acetyl amino acids
    • Fauchere J.L., and Pliska V. Hydrophobic parameter π of amino-acid side chains from the partitioning of N-acetyl amino acids. Eur. J. Med. Chem. 18 (1983) 369-375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.