Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

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http://www.wikidata.org/entity/Q40043667
The positively charged surface of herpes simplex virus UL42 mediates DNA binding.Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisEvidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interfaceCloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.Lobucavir is phosphorylated in human cytomegalovirus-infected and -uninfected cells and inhibits the viral DNA polymeraseBipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory functionThe catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateTwo regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches.Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein UL44 are crucial for interaction with the UL54 catalytic subunit.Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit.Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain.Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44
P2860

Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

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http://www.wikidata.org/entity/Q40043667
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Mutations in the C terminus of ...... ing basal polymerase activity.
@en
type
label
Mutations in the C terminus of ...... ing basal polymerase activity.
@en
prefLabel
Mutations in the C terminus of ...... ing basal polymerase activity.
@en
P1433
P1476
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P932
P1433
P1476
Mutations in the C terminus of ...... ting basal polymerase activity
@en
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P932