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

Benzer Materyaller

• 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
  Yazar:: Weisshart, Klaus, ve diğerleri
  Baskı/Yayın Bilgisi: (1999)
• Translational regulation of herpes simplex virus DNA polymerase.
  Yazar:: Yager, D R, ve diğerleri
  Baskı/Yayın Bilgisi: (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
  Yazar:: Weisshart, Klaus, ve diğerleri
  Baskı/Yayın Bilgisi: (2006)
• The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
  Yazar:: Digard, P, ve diğerleri
  Baskı/Yayın Bilgisi: (1993)
• Inhibition of Translation by a Short Element in the 5′ Leader of the Herpes Simplex Virus 1 DNA Polymerase Transcript
  Yazar:: Bryant, Kevin F., ve diğerleri
  Baskı/Yayın Bilgisi: (2008)