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Volumn 314, Issue 1-2, 2003, Pages 191-199

Frameshift mutation events in β-glucosidases

Author keywords

Compensated frameshift mutation; Molecular evolution; O glycoside hydrolases; Reading frame; Sequence alignment

Indexed keywords

BETA GLUCOSIDASE;

EID: 0141760282     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00828-X     Document Type: Article
Times cited : (3)

References (24)
  • 1
    • 0034666315 scopus 로고    scopus 로고
    • Increased thermal resistance and modification of the catalytic properties of a beta-glucosidase by random mutagenesis and in vitro recombination
    • Arrizubieta M.J., Polaina J. Increased thermal resistance and modification of the catalytic properties of a beta-glucosidase by random mutagenesis and in vitro recombination. J. Biol. Chem. 275:2000;28843-28848.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28843-28848
    • Arrizubieta, M.J.1    Polaina, J.2
  • 2
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A. The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure. 3:1995;951-960.
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 4
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • H.J. Gilbert, G. Davies, B. Henrissat, & B. Svensson. Cambridge: The Royal Society of Chemistry
    • Coutinho P.M., Henrissat B. Carbohydrate-active enzymes: an integrated database approach. Gilbert H.J., Davies G., Henrissat B., Svensson B. Recent Advances in Carbohydrate Bioengineering. 1999;3-12 The Royal Society of Chemistry, Cambridge.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 5
    • 0001849438 scopus 로고    scopus 로고
    • The modular structure of cellulases and other carbohydrate-active enzymes: An integrated database approach
    • K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita, & T. Kimura. Tokyo: Uni Publishers
    • Coutinho P.M., Henrissat B. The modular structure of cellulases and other carbohydrate-active enzymes: an integrated database approach. Ohmiya K., Hayashi K., Sakka K., Kobayashi Y., Karita S., Kimura T. Genetics, Biochemistry and Ecology of Cellulose Degradation. 1999;15-23 Uni Publishers, Tokyo.
    • (1999) Genetics, Biochemistry and Ecology of Cellulose Degradation , pp. 15-23
    • Coutinho, P.M.1    Henrissat, B.2
  • 8
    • 0027273838 scopus 로고
    • Kinetic characterization of a beta-glucosidase from a yeast, Candida wickerhamii
    • Freer S.N. Kinetic characterization of a beta-glucosidase from a yeast, Candida wickerhamii. J. Biol. Chem. 268:1993;9337-9342.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9337-9342
    • Freer, S.N.1
  • 9
    • 0346055862 scopus 로고    scopus 로고
    • Circular permutants in beta-glucosidases (family 3) within a predicted double-domain topology that includes a (beta/alpha)8-barrel
    • Garcia-Vallve S., Rojas A., Palau J., Romeu A. Circular permutants in beta-glucosidases (family 3) within a predicted double-domain topology that includes a (beta/alpha)8-barrel. Proteins. 31:1998;214-223.
    • (1998) Proteins , vol.31 , pp. 214-223
    • Garcia-Vallve, S.1    Rojas, A.2    Palau, J.3    Romeu, A.4
  • 12
    • 0004345433 scopus 로고    scopus 로고
    • Genetics. Analysis of Genes and Genomes
    • Boston: Jones and Bartlett Publishers
    • Hartl D.L., Jones E.W. Genetics. Analysis of Genes and Genomes. 5th ed. 2000;Jones and Bartlett Publishers, Boston.
    • (2000) 5th ed.
    • Hartl, D.L.1    Jones, E.W.2
  • 13
    • 0034333059 scopus 로고    scopus 로고
    • Comparative modelling of the three-dimensional structures of family 3 glycoside hydrolases
    • Harvey A.J., Hrmova M., De Gori R., Varghese J.N., Fincher G.B. Comparative modelling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins. 41:2000;257-269.
    • (2000) Proteins , vol.41 , pp. 257-269
    • Harvey, A.J.1    Hrmova, M.2    De Gori, R.3    Varghese, J.N.4    Fincher, G.B.5
  • 14
    • 0027414603 scopus 로고
    • Hidden domains and active site residues in beta-glycanase-encoding gene sequences?
    • Henrissat B. Hidden domains and active site residues in beta-glycanase-encoding gene sequences? Gene. 125:1993;199-204.
    • (1993) Gene , vol.125 , pp. 199-204
    • Henrissat, B.1
  • 15
  • 17
    • 0003421005 scopus 로고    scopus 로고
    • Sunderland Massachusetts: Sinuauer Associates, Publishers
    • Li W.H. Molecular Evolution. 1997;Sinuauer Associates, Publishers, Sunderland Massachusetts.
    • (1997) Molecular Evolution
    • Li, W.H.1
  • 18
    • 0026434573 scopus 로고
    • Finding DNA sequencing errors
    • Roberts L. Finding DNA sequencing errors. Science. 252:1991;1255-1256.
    • (1991) Science , vol.252 , pp. 1255-1256
    • Roberts, L.1
  • 19
    • 85031061975 scopus 로고    scopus 로고
    • 3′Flanking region of a family 1 beta-glucosidase
    • Rojas A., Romeu A. 3′Flanking region of a family 1 beta-glucosidase. Biochem. J. 320:1996;693-694.
    • (1996) Biochem. J. , vol.320 , pp. 693-694
    • Rojas, A.1    Romeu, A.2
  • 20
    • 0029960050 scopus 로고    scopus 로고
    • The HSSP database of protein structure sequence alignments
    • Schneider R., Sander C. The HSSP database of protein structure sequence alignments. Nucleic Acids Res. 24:1996;201-205.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 201-205
    • Schneider, R.1    Sander, C.2
  • 21
    • 0026063030 scopus 로고
    • Molecular sequence accuracy and the analysis of protein coding regions
    • States D.J., Botstein D. Molecular sequence accuracy and the analysis of protein coding regions. Proc. Natl. Acad. Sci. U. S. A. 88:1991;5518-5522.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5518-5522
    • States, D.J.1    Botstein, D.2
  • 22
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 23
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese J.N., Hrmova M., Fincher G.B. Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure. 7:1999;179-190.
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.