Pages that link to "Q35850793"

The following pages link to Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42 (Q35850793):

Displaying 22 items.

• Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha (Q24652672) (← links)
• The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase (Q27625216) (← links)
• Crystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1 (Q27657653) (← links)
• Inhibition of Epstein-Barr virus replication by a benzimidazole L-riboside: novel antiviral mechanism of 5, 6-dichloro-2-(isopropylamino)-1-beta-L-ribofuranosyl-1H-benzimidazole (Q28343493) (← links)
• Hopping of a processivity factor on DNA revealed by single-molecule assays of diffusion (Q30483015) (← links)
• 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. (Q33638763) (← links)
• Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis (Q33756104) (← links)
• The human cytomegalovirus UL44 C clamp wraps around DNA. (Q33885011) (← links)
• The positively charged surface of herpes simplex virus UL42 mediates DNA binding (Q33929077) (← links)
• 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 (Q33987437) (← links)
• Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42. (Q34348919) (← links)
• A tale of two HSV-1 helicases: roles of phage and animal virus helicases in DNA replication and recombination (Q34408074) (← links)
• The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: implications for a dual role as a primer recognition factor and processivity clamp (Q36423471) (← links)
• A novel processive mechanism for DNA synthesis revealed by structure, modeling and mutagenesis of the accessory subunit of human mitochondrial DNA polymerase (Q36435827) (← links)
• Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity (Q37256683) (← links)
• Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated (Q38302175) (← links)
• Herpesvirus DNA polymerases: Structures, functions and inhibitors (Q39116341) (← links)
• Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches (Q39606081) (← links)
• A novel strategy to engineer DNA polymerases for enhanced processivity and improved performance in vitro (Q40695789) (← links)
• Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis (Q41979659) (← links)
• 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 (Q42797357) (← links)
• Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor (Q77086710) (← links)