Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain.

Ítems similars

• 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.
  per: Tenney, D J, et al.
  Publicat: (1993)
• Functional analysis of the herpes simplex virus UL42 protein.
  per: Digard, P, et al.
  Publicat: (1993)
• The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
  per: Digard, P, et al.
  Publicat: (1993)
• The Positively Charged Surface of Herpes Simplex Virus UL42 Mediates DNA Binding
  per: Komazin-Meredith, Gloria, et al.
  Publicat: (2008)
• Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype.
  per: Johnson, P A, et al.
  Publicat: (1991)