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Volumn 12, Issue 8, 2003, Pages 1686-1693

Library analysis of SCHEMA-guided protein recombination

Author keywords

Chimera; Directed evolution; Lactamase; PSE 4; Recombination; Schema; TEM 1

Indexed keywords

BETA LACTAMASE; CHIMERIC PROTEIN; M PROTEIN; PEPTIDE LIBRARY; PROTEIN PSE4; PROTEIN TEM1; RECOMBINANT DNA; UNCLASSIFIED DRUG;

EID: 0038731100     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0306603     Document Type: Article
Times cited : (131)

References (27)
  • 2
    • 0035843136 scopus 로고    scopus 로고
    • Combinatorial and computational challenges for biocatalyst design
    • -. 2001b. Combinatorial and computational challenges for biocatalyst design. Nature 409: 253-257.
    • (2001) Nature , vol.409 , pp. 253-257
  • 4
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., Raillard, S.A., Bermudez, E., and Stemmer, W.P. 1998. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391: 288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.4
  • 5
    • 0035854021 scopus 로고    scopus 로고
    • Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling
    • Gibbs, M.D., Nevalainen, K.M., and Bergquist, P.L. 2001. Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling. Gene 271: 13-20.
    • (2001) Gene , vol.271 , pp. 13-20
    • Gibbs, M.D.1    Nevalainen, K.M.2    Bergquist, P.L.3
  • 6
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M.C. 1997. SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 7
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K., and Pease, L.R. 1989. Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension. Gene 77: 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
  • 8
    • 0027275788 scopus 로고
    • Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution
    • Jelsch, C., Mourey, L., Masson, J.M., and Samama, J.P. 1993. Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution. Proteins 16: 364-383.
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Masson, J.M.3    Samama, J.P.4
  • 9
    • 0036307433 scopus 로고    scopus 로고
    • Analysis of shuffled gene libraries
    • Joern, J.M., Meinhold, P., and Arnold, F.H. 2002. Analysis of shuffled gene libraries. J. Mol. Biol. 316: 643-656.
    • (2002) J. Mol. Biol. , vol.316 , pp. 643-656
    • Joern, J.M.1    Meinhold, P.2    Arnold, F.H.3
  • 10
    • 0035895310 scopus 로고    scopus 로고
    • Insights into the molecular basis for the carbenicillinase activity of PSE-4 β-lactamase from crystallographic and kinetic studies
    • Lim, D., Sanschagrin, F., Passmore, L., De Castro, L., Levesque, R.C., and Strynadka, N.C. 2001. Insights into the molecular basis for the carbenicillinase activity of PSE-4 β-lactamase from crystallographic and kinetic studies. Biochemistry 40: 395-402.
    • (2001) Biochemistry , vol.40 , pp. 395-402
    • Lim, D.1    Sanschagrin, F.2    Passmore, L.3    De Castro, L.4    Levesque, R.C.5    Strynadka, N.C.6
  • 12
    • 0032032930 scopus 로고    scopus 로고
    • Catalytic properties of class A β-lactamases: Efficiency and diversity
    • Matagne, A., Lamotte-Brasseur, J., and Frere, J.M. 1998. Catalytic properties of class A β-lactamases: Efficiency and diversity. Biochem. J. 330: 581-598.
    • (1998) Biochem. J. , vol.330 , pp. 581-598
    • Matagne, A.1    Lamotte-Brasseur, J.2    Frere, J.M.3
  • 13
    • 0042815927 scopus 로고    scopus 로고
    • Analysis of shuffled libraries by oligonucleotide probe hybridization
    • Meinhold, P., Joern, J., and Silberg, J.J. 2003. Analysis of shuffled libraries by oligonucleotide probe hybridization, Methods Mol. Biol. 231: 177-188.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 177-188
    • Meinhold, P.1    Joern, J.2    Silberg, J.J.3
  • 14
  • 15
    • 0031587291 scopus 로고    scopus 로고
    • Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences
    • Moore, J.C., Jin, H.M., Kuchner, O., and Arnold, F.H. 1997. Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences. J. Mol. Biol. 272: 336-347.
    • (1997) J. Mol. BioL. , vol.272 , pp. 336-347
    • Moore, J.C.1    Jin, H.M.2    Kuchner, O.3    Arnold, F.H.4
  • 16
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille, P., Bakhtina, M., and Tsai, M. 2002. Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol. 321: 677.
    • (2002) J. Mol. Biol. , vol.321 , pp. 677
    • O'Maille, P.1    Bakhtina, M.2    Tsai, M.3
  • 17
    • 0033770720 scopus 로고    scopus 로고
    • Evolution of protein function by domain swapping
    • Ostermeier, M. and Benkovic, S.J. 2001. Evolution of protein function by domain swapping. Adv. Protein Chem. 55: 29-77.
    • (2001) Adv. Protein Chem. , vol.55 , pp. 29-77
    • Ostermeier, M.1    Benkovic, S.J.2
  • 18
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier, M., Shim, J.H., and Benkovic, S.J. 1999. A combinatorial approach to hybrid enzymes independent of DNA homology. Nat. Biotechnol. 17: 1205-1209.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 19
    • 0344474600 scopus 로고    scopus 로고
    • Characterization of a PSE-4 mutant with different properties in relation to penicillanic acid sulfones: Importance of residues 216 to 218 in class A β-lactamases
    • Sabbagh, Y., Theriault, E., Sanschagrin, F., Voyer, N., Palzkill, T., and Levesque, R.C. 1998. Characterization of a PSE-4 mutant with different properties in relation to penicillanic acid sulfones: Importance of residues 216 to 218 in class A β-lactamases. Antimicrob. Agents Chemother. 42: 2319-2325.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2319-2325
    • Sabbagh, Y.1    Theriault, E.2    Sanschagrin, F.3    Voyer, N.4    Palzkill, T.5    Levesque, R.C.6
  • 20
    • 0034018940 scopus 로고    scopus 로고
    • Structure-function analysis of α-helix H4 using PSE-4 as a model enzyme representative of class A β-lactamases
    • Savoie, A., Sanschagrin, F., Palzkill, T., Voyer, N., and Levesque, R.C. 2000. Structure-function analysis of α-helix H4 using PSE-4 as a model enzyme representative of class A β-lactamases. Protein Eng. 13: 267-274.
    • (2000) Protein Eng. , vol.13 , pp. 267-274
    • Savoie, A.1    Sanschagrin, F.2    Palzkill, T.3    Voyer, N.4    Levesque, R.C.5
  • 21
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber, V., Martinez, C.A., and Arnold, F.H. 2001. Libraries of hybrid proteins from distantly related sequences. Nat. Biotechnol. 19: 456-460.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 23
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W.P. 1994a. DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. 91: 10747-10751.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 24
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • -. 1994b. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370: 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
  • 26
    • 0033567665 scopus 로고    scopus 로고
    • Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair
    • Volkov, A.A., Shao, Z., and Arnold, F.H. 1999. Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair. Nucleic Acids Res. 27: e18.
    • (1999) Nucleic Acids Res. , vol.27
    • Volkov, A.A.1    Shao, Z.2    Arnold, F.H.3
  • 27
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L., Shao, Z., Affholter, J.A., and Arnold, F.H. 1998. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol. 16: 258-261.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.