Solution Structure of the C-terminal Domain of A20, the Missing Brick for the Characterization of the Interface between Vaccinia Virus DNA Polymerase and its Processivity Factor

Author:

Bersch Beate,Tarbouriech Nicolas,Burmeister Wim P.,Iseni Frédéric

Funder

French National Research Agency

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference42 articles.

1. Moss, B. (2013). Poxviridae. In Fields Virol. 2 (Fields, B.M., Knipe, D.M. & Howley, P.M. eds), Wolters Kluwer Health/Lippincott Williams & Wilkins, Philadelphia, pp. 2129–2159.

2. Identification of a poxvirus gene encoding a uracil DNA glycosylase;Upton;Proc. Natl. Acad. Sci. USA,1993

3. Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme;Boyle;J. Biol. Chem.,2011

4. Biochemical and genetic analysis of the vaccinia virus D5 protein: multimerization-dependent ATPase activity is required to support viral DNA replication;Boyle;J. Virol.,2007

5. Poxvirus DNA primase;De Silva;Proc. Natl. Acad. Sci. USA,2007

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