Functional Interaction between the Herpes Simplex Virus Type 1 Polymerase Processivity Factor and Origin-Binding Proteins: Enhancement of UL9 Helicase Activity

Ítems similars

• The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA
  per: Trego, Kelly S., et al.
  Publicat: (2005)
• Helicase Motif Ia Is Involved in Single-Strand DNA-Binding and Helicase Activities of the Herpes Simplex Virus Type 1 Origin-Binding Protein, UL9
  per: Marintcheva, Boriana, et al.
  Publicat: (2003)
• Evidence against a Simple Tethering Model for Enhancement of Herpes Simplex Virus DNA Polymerase Processivity by Accessory Protein UL42
  per: Chaudhuri, Murari, et al.
  Publicat: (2002)
• 3′ to 5′ Exonuclease Activity of Herpes Simplex Virus Type 1 DNA Polymerase Modulates Its Strand Displacement Activity
  per: Zhu, Yali, et al.
  Publicat: (2003)
• The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for function.
  per: Martinez, R, et al.
  Publicat: (1992)