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One or more keywords matched the following items that are connected to Coen, Donald
Item TypeName
Academic Article Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches.
Academic Article Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor.
Academic Article Hopping of a processivity factor on DNA revealed by single-molecule assays of diffusion.
Academic Article The herpes simplex virus processivity factor, UL42, binds DNA as a monomer.
Academic Article Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42.
Academic Article Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity.
Academic Article Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase.
Academic Article Functional analysis of the herpes simplex virus UL42 protein.
Academic Article Mutational analysis of DNA polymerase substrate recognition and subunit interactions using herpes simplex virus as prototype.
Academic Article The pre-NH(2)-terminal domain of the herpes simplex virus 1 DNA polymerase catalytic subunit is required for efficient viral replication.
Academic Article The positively charged surface of herpes simplex virus UL42 mediates DNA binding.
Academic Article Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.
Academic Article Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface.
Academic Article 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.
Academic Article The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase.
Academic Article Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis.
Academic Article The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
Academic Article Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis.
Academic Article Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site.
Academic Article Identification of a small molecule that inhibits herpes simplex virus DNA Polymerase subunit interactions and viral replication.
Academic Article Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replication.
Academic Article Inhibition of translation by a short element in the 5' leader of the herpes simplex virus 1 DNA polymerase transcript.
Academic Article Structural and functional organization of herpes simplex virus DNA polymerase investigated by limited proteolysis.
Academic Article Pathogenicity of herpes simplex virus mutants containing drug resistance mutations in the viral DNA polymerase gene.
Concept Exodeoxyribonucleases
Academic Article Roles of conserved residues within the pre-NH2-terminal domain of herpes simplex virus 1 DNA polymerase in replication and latency in mice.
Academic Article Herpes Simplex Virus 1 DNA Polymerase RNase H Activity Acts in a 3'-to-5' Direction and Is Dependent on the 3'-to-5' Exonuclease Active Site.
Academic Article HSV-1 DNA polymerase 3'-5' exonuclease-deficient mutant D368A exhibits severely reduced viral DNA synthesis and polymerase expression.
Search Criteria
  • Exodeoxyribonucleases
Funded by the NIH National Center for Advancing Translational Sciences through its Clinical and Translational Science Awards Program, grant number UL1TR002541.