Conserved cysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation of the DNA-binding activity in vitro.

Antzeko izenburuak

• The carboxy-terminal domain shared by the bovine papillomavirus E2 transactivator and repressor proteins contains a specific DNA binding activity.
  nork: McBride, A A, et al.
  Argitaratua: (1988)
• E2 polypeptides encoded by bovine papillomavirus type 1 form dimers through the common carboxyl-terminal domain: transactivation is mediated by the conserved amino-terminal domain.
  nork: McBride, A A, et al.
  Argitaratua: (1989)
• Evolutionary conservation of DNA-contact residues in DNA-binding domains
  nork: Chang, Yao-Lin, et al.
  Argitaratua: (2008)
• The conserved redox-sensitive cysteine residue of the DNA-binding region in the c-Rel protein is involved in the regulation of the phosphorylation of the protein.
  nork: Glineur, C, et al.
  Argitaratua: (2000)
• Surface Mutagenesis of the Bovine Papillomavirus E1 DNA Binding Domain Reveals Residues Required for Multiple Functions Related to DNA Replication
  nork: Schuck, Stephen, et al.
  Argitaratua: (2006)