The UL8 Subunit of the Herpes Simplex Virus Type-1 DNA Helicase-Primase Optimizes Utilization of DNA Templates Covered by the Homologous Single-strand DNA-binding Protein ICP8

This publication has 13 references indexed in Scilit:

• MECHANISMS OF HELICASE-CATALYZED DNA UNWINDING
  Annual Review of Biochemistry, 1996
• Visualization of the Unwinding of Long DNA Chains by the Herpes Simplex Virus Type 1 UL9 Protein and ICP8
  Journal of Molecular Biology, 1996
• ESCHERICHIA COLI SINGLE-STRANDED DNA-BINDING PROTEIN: Multiple DNA-Binding Modes and Cooperativities
  Annual Review of Biochemistry, 1994
• Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.
  Proceedings of the National Academy of Sciences, 1993
• Purification and properties of the herpes simplex virus type 1 UL8 protein
  Journal of General Virology, 1993
• Herpes simplex virus-1 helicase-primase
  Published by Elsevier ,1991
• Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products.
  Proceedings of the National Academy of Sciences, 1991
• Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities
  Nucleic Acids Research, 1990
• Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products.
  Proceedings of the National Academy of Sciences, 1989
• Mutations in the herpes simplex virus major DNA-binding protein gene leading to altered sensitivity to DNA polymerase inhibitors
  Virology, 1985