Thioredoxin, the Processivity Factor, Sequesters an Exposed Cysteine in the Thumb Domain of Bacteriophage T7 DNA Polymerase

Lignende værker

• Conformational dynamics of bacteriophage T7 DNA polymerase and its processivity factor, Escherichia coli thioredoxin
  af: Akabayov, Barak, et al.
  Udgivet: (2010)
• Zinc-binding Domain of the Bacteriophage T7 DNA Primase Modulates Binding to the DNA Template
  af: Lee, Seung-Joo, et al.
  Udgivet: (2012)
• DNA Recognition by the DNA Primase of Bacteriophage T7: A Structure#Function Study of the Zinc-Binding Domain DNA Recognition by the DNA Primase of Bacteriophage T7: A Structure–Function Study of the Zinc-Binding Domain
  af: Akabayov, Barak, et al.
  Udgivet: (2009)
• Binding of Mn-deoxyribonucleoside triphosphates to the active site of the DNA polymerase of bacteriophage T7
  af: Akabayov, Barak, et al.
  Udgivet: (2011)
• The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I
  af: Bedford, Ella, et al.
  Udgivet: (1997)