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Volumn 70, Issue 7, 1996, Pages 4816-4818

Evidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3′-5′ exonuclease

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; NUCLEASE; PHOSPHODIESTERASE I;

EID: 0029992358     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.7.4816-4818.1996     Document Type: Article
Times cited : (10)

References (11)
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    • Blanco, L.1    Bernad, A.2    Blasco, M.A.3    Salas, M.4
  • 2
    • 0024793120 scopus 로고
    • Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5′-3′ exonuclease with ribonuclease H activity
    • Crute, J. J., and I. R. Lehman. 1989. Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5′-3′ exonuclease with ribonuclease H activity. J. Biol. Chem. 264:19266-19270.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19266-19270
    • Crute, J.J.1    Lehman, I.R.2
  • 3
    • 0025253822 scopus 로고
    • The herpes simplex virus type 1 UL42 gene product: A subunit of DNA polymerase that functions to increase processivity
    • Gotllieb, J., A. I. Marcy, D. M. Coen, and M. D. Challberg. 1990. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity. J. Virol. 64:5976-5987.
    • (1990) J. Virol. , vol.64 , pp. 5976-5987
    • Gotllieb, J.1    Marcy, A.I.2    Coen, D.M.3    Challberg, M.D.4
  • 4
    • 0029585446 scopus 로고
    • Mutations within conserved motifs in the 3′-5′ exonuclease domain of herpes simplex virus DNA polymerase
    • Hall, J. D., K. L. Orth, K. L. Sander, B. M. Swihart, and R. A. Senese. 1995. Mutations within conserved motifs in the 3′-5′ exonuclease domain of herpes simplex virus DNA polymerase. J. Gen. Virol. 76:2999-3008.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2999-3008
    • Hall, J.D.1    Orth, K.L.2    Sander, K.L.3    Swihart, B.M.4    Senese, R.A.5
  • 5
    • 0002537042 scopus 로고
    • Herpes simplex virus type 1 DNA polymerase: Eukaryotic model enzyme and principal target of antiviral therapy
    • Y. Becker and G. Darai (ed.), Springer-Verlag, Berlin
    • Knopf, C. W., and R. Strick. 1994. Herpes simplex virus type 1 DNA polymerase: Eukaryotic model enzyme and principal target of antiviral therapy, p. 87-135. In Y. Becker and G. Darai (ed.), Frontiers of virology, vol. 3. Springer-Verlag, Berlin.
    • (1994) Frontiers of Virology , vol.3 , pp. 87-135
    • Knopf, C.W.1    Strick, R.2
  • 6
    • 0025299332 scopus 로고
    • Comparison of exonucleolytic activities of herpes simplex virus type-1 DNA polymerase and DNase
    • Knopf, C. W., and K. Weisshart. 1990. Comparison of exonucleolytic activities of herpes simplex virus type-1 DNA polymerase and DNase. Eur. J. Biochem. 191:263-273.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 263-273
    • Knopf, C.W.1    Weisshart, K.2
  • 7
    • 0018770603 scopus 로고
    • Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity
    • Knopf, K.-W. 1979. Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity. Eur. J. Biochem. 98: 231-244.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 231-244
    • Knopf, K.-W.1
  • 8
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    • Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells
    • Marcy, A. I., P. D. Olivo, M. D. Challberg, and D. M. Coen. 1990. Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells. Nucleic Acids Res. 18: 1207-1215.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1207-1215
    • Marcy, A.I.1    Olivo, P.D.2    Challberg, M.D.3    Coen, D.M.4
  • 10
    • 0023785209 scopus 로고
    • The herpes simplex virus type 1 DNA polymerase. Polypeptide structure and antigenic domains
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  • 11
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    • Weisshart, K., A. A. Kuo, C. B. C. Hwang, K. Kumura, and D. M. Coen. 1994. Structural and functional organization of herpes simplex virus DNA polymerase investigated by limited proteolysis. J. Biol. Chem. 269:22788-22796.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22788-22796
    • Weisshart, K.1    Kuo, A.A.2    Hwang, C.B.C.3    Kumura, K.4    Coen, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.