Stanitsa, Eleni S <br/><br/>
Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase.  [electronic resource] 

 -  The Journal of biological chemistry  Feb 2006 
 - 3439-51 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M511239200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Bacteriophage M13--metabolism<br/>Blotting, Southern<br/>Catalysis<br/>Cell Line<br/>Chlorocebus aethiops<br/>Chromatography<br/>Cytoplasm--metabolism<br/>DNA Replication<br/>DNA, Viral--metabolism<br/>DNA-Directed DNA Polymerase--chemistry<br/>Dimerization<br/>Epitopes--chemistry<br/>Humans<br/>Immunoblotting<br/>Immunoprecipitation<br/>In Vitro Techniques<br/>Mutation<br/>Open Reading Frames<br/>Phenotype<br/>Plasmids--metabolism<br/>Protein Binding<br/>Protein Biosynthesis<br/>Protein Interaction Mapping<br/>Silver Staining<br/>Software<br/>Temperature<br/>Transcription, Genetic<br/>Uracil--chemistry<br/>Uracil-DNA Glycosidase--chemistry<br/>Vaccinia virus--enzymology