Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism-Reference-Cited by-同舟云学术

Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism

Published:2007-07 Issue:14 Volume:35 Page:4779-4791
ISSN:1362-4962
Container-title:Nucleic Acids Research
language:en
Short-container-title:

Author:

Loregian Arianna,Sinigalia Elisa,Mercorelli Beatrice,Palù Giorgio,Coen Donald M.

Publisher

Oxford University Press (OUP)

Subject

Genetics

Link

http://academic.oup.com/nar/article-pdf/35/14/4779/16762951/gkm506.pdf

Reference47 articles.

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2. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA;Krishna;Cell,1994

3. Clamp loaders and sliding clamps;Jeruzalmi;Curr. Opin. Struct. Biol,2002

4. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer;Randell;J. Mol. Biol,2004

5. 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;Weisshart;J. Virol,1999

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