Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

Samankaltaisia teoksia

• Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain.
  Tekijä: Tenney, D J, et al.
  Julkaistu: (1993)
• 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 extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
  Tekijä: Digard, P, et al.
  Julkaistu: (1993)
• 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)
• Evidence against a Simple Tethering Model for Enhancement of Herpes Simplex Virus DNA Polymerase Processivity by Accessory Protein UL42
  Tekijä: Chaudhuri, Murari, et al.
  Julkaistu: (2002)