Identification of Crucial Hydrogen-Bonding Residues for the Interaction of Herpes Simplex Virus DNA Polymerase Subunits via Peptide Display, Mutational, and Calorimetric Approaches

Samankaltaisia teoksia

• 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
  Tekijä: Weisshart, Klaus, et al.
  Julkaistu: (1999)
• Translational regulation of herpes simplex virus DNA polymerase.
  Tekijä: Yager, D R, et al.
  Julkaistu: (1990)
• 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
  Tekijä: Weisshart, Klaus, et al.
  Julkaistu: (2006)
• 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 Translation by a Short Element in the 5′ Leader of the Herpes Simplex Virus 1 DNA Polymerase Transcript
  Tekijä: Bryant, Kevin F., et al.
  Julkaistu: (2008)