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

Eitemau Tebyg

• 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)
• Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42.
  gan: Chow, C S, et al.
  Cyhoeddwyd: (1995)
• Functional analysis of the herpes simplex virus UL42 protein.
  gan: Digard, P, et al.
  Cyhoeddwyd: (1993)
• Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template.
  gan: Gottlieb, J, et al.
  Cyhoeddwyd: (1994)
• The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
  gan: Digard, P, et al.
  Cyhoeddwyd: (1993)