The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.

Eitemau Tebyg

• Functional analysis of the herpes simplex virus UL42 protein.
  gan: Digard, P, et al.
  Cyhoeddwyd: (1993)
• Herpes Simplex Virus Processivity Factor UL42 Imparts Increased DNA-Binding Specificity to the Viral DNA Polymerase and Decreased Dissociation from Primer-Template without Reducing the Elongation Rate
  gan: Weisshart, Klaus, et al.
  Cyhoeddwyd: (1999)
• Herpes Simplex Virus Processivity Factor UL42 Imparts Increased DNA-Binding Specificity to the Viral DNA Polymerase and Decreased Dissociation from Primer-Template without Reducing the Elongation Rate
  gan: Weisshart, Klaus, et al.
  Cyhoeddwyd: (2006)
• Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication.
  gan: Stow, N D
  Cyhoeddwyd: (1993)
• Herpes Simplex Virus Mutants with Multiple Substitutions Affecting DNA Binding of UL42 Are Impaired for Viral Replication and DNA Synthesis
  gan: Jiang, Changying, et al.
  Cyhoeddwyd: (2007)