Evidence against a Simple Tethering Model for Enhancement of Herpes Simplex Virus DNA Polymerase Processivity by Accessory Protein UL42

Samankaltaisia teoksia

• Functional Interaction between the Herpes Simplex Virus Type 1 Polymerase Processivity Factor and Origin-Binding Proteins: Enhancement of UL9 Helicase Activity
  Tekijä: Trego, Kelly S., et al.
  Julkaistu: (2003)
• Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template.
  Tekijä: Gottlieb, J, et al.
  Julkaistu: (1994)
• 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
  Tekijä: Trego, Kelly S., et al.
  Julkaistu: (2005)
• Inhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecific.
  Tekijä: Owsianka, A M, et al.
  Julkaistu: (1993)
• Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.
  Tekijä: Monahan, S J, et al.
  Julkaistu: (1993)