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Volumn 5, Issue 9, 1997, Pages 1129-1134

Helicase structures: A new twist on DNA unwinding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); HEPATITIS C VIRUS;

EID: 0031572286     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00263-3     Document Type: Review
Times cited : (23)

References (13)
  • 2
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T.M. & Bjornson, K.P. (1996). Mechanisms of helicase-catalyzed DNA unwinding. Ann. Rev. Biochem. 65, 169-214.
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 3
    • 0017113549 scopus 로고
    • Enzymic unwinding of DNA 2. Chain separation by an ATP-dependent DNA unwinding enzyme
    • Abdel-Monhem, M., Dürwald, H. & Hoffmann-Berling, H. (1976). Enzymic unwinding of DNA 2. Chain separation by an ATP-dependent DNA unwinding enzyme. Eur. J. Biochem. 65, 441-449.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 441-449
    • Abdel-Monhem, M.1    Dürwald, H.2    Hoffmann-Berling, H.3
  • 4
    • 0017332435 scopus 로고
    • A mechanism of duplex DNA replication revealed by enzymatic studies of phage X174: Catalytic strand separation in advance of replication
    • Scott, J.F., Eisenberg, S., Bertsch, L.L. & Kornberg, A. (1977). A mechanism of duplex DNA replication revealed by enzymatic studies of phage X174: catalytic strand separation in advance of replication. Proc. Natl. Acad. Sci. USA 74, 193-197.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 193-197
    • Scott, J.F.1    Eisenberg, S.2    Bertsch, L.L.3    Kornberg, A.4
  • 7
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swivelling revealed by the crystal structures of binary and ternary complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., Hsieh, J., Gauss, G.H., Lohman, T.M. & Waksman, G. (1997). Major domain swivelling revealed by the crystal structures of binary and ternary complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90, 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 8
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A.E. & Koonin, E.V., (1993). Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 9
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982). Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 10
    • 10144248959 scopus 로고    scopus 로고
    • A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III
    • Brosh, R.M., Jr. & Matson, S.W. (1996). A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III. J. Biol. Chem. 271, 25630-25638.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25630-25638
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 11
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong, I. & Lohman, T.M. (1992). Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256, 350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 12
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali, J.A. & Lohman, T.M. (1997). Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275, 377-380.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 13
    • 0027237279 scopus 로고
    • Heterodimer formation between Escherichia coli Rep and UvrD proteins
    • Wong, I., Amaratunga, M. & Lohman, T.M. (1993). Heterodimer formation between Escherichia coli Rep and UvrD proteins. J. Biol. Chem. 268, 20386-20391.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20386-20391
    • Wong, I.1    Amaratunga, M.2    Lohman, T.M.3


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