The Herpes Simplex Virus Processivity Factor, UL42, Binds DNA as a Monomer
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference12 articles.
1. Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5′–3′ exonuclease with ribonuclease H activity;Crute;J. Biol. Chem.,1989
2. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity;Gottlieb;J. Virol.,1990
3. Purification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein: properties of the protein and evidence of its association with the virus-encoded DNA polymerase;Gallo;J. Virol.,1988
4. The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase;Zuccola;Mol. Cell,2000
5. Mammalian DNA polymerase auxiliary proteins: analysis of replication factor C-catalyzed proliferating cell nuclear antigen loading onto circular double-stranded DNA;Podust;Mol. Cell. Biol.,1995
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