Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities.
about
Mechanism and evolution of DNA primasesInitiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alphaThe DNA helicase-primase complex as a target for herpes viral infectionInhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the UL5-UL8-UL52 complexReplication of herpes simplex virus DNA.An intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity.Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.Human cytomegalovirus UL102 geneThe 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.Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.The UL5 gene of herpes simplex virus type 1: isolation of a lacZ insertion mutant and association of the UL5 gene product with other members of the helicase-primase complex.The six conserved helicase motifs of the UL5 gene product, a component of the herpes simplex virus type 1 helicase-primase, are essential for its function.Herpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication originThe UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.Interaction of herpes primase with the sugar of a NTP.Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activityAssociation of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products.Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays.Sequence-dependent primer synthesis by the herpes simplex virus helicase-primase complex.The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding.A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.trans-acting requirements for replication of Epstein-Barr virus ori-Lyt.Interactions of a subassembly of the herpes simplex virus type 1 helicase-primase with DNA.Herpes simplex virus-1 helicase-primase: roles of each subunit in DNA binding and phosphodiester bond formation.UL52 primase interactions in the herpes simplex virus 1 helicase-primase are affected by antiviral compounds and mutations causing drug resistanceEleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA replication.Association between the herpes simplex virus major DNA-binding protein and alkaline nuclease.The UL8 subunit of the helicase/primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication.The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single strand DNA-binding protein (ICP8)-coated DNA substrates.Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding.Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase.The UL8 subunit of the herpes simplex virus type-1 DNA helicase-primase optimizes utilization of DNA templates covered by the homologous single-strand DNA-binding protein ICP8.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Identification of conserved amino acids in the herpes simplex virus type 1 UL8 protein required for DNA synthesis and UL52 primase interaction in the virus replisome.ASP2151, a novel helicase-primase inhibitor, possesses antiviral activity against varicella-zoster virus and herpes simplex virus types 1 and 2.Template recognition and ribonucleotide specificity of the DNA primase of bacteriophage T7.Identification of the primase active site of the herpes simplex virus type 1 helicase-primase.
P2860
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P2860
Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Herpes simplex virus helicase- ...... e and DNA helicase activities.
@en
type
label
Herpes simplex virus helicase- ...... e and DNA helicase activities.
@en
prefLabel
Herpes simplex virus helicase- ...... e and DNA helicase activities.
@en
P2860
P356
P1476
Herpes simplex virus helicase- ...... e and DNA helicase activities.
@en
P2093
P2860
P304
P356
10.1093/NAR/18.12.3573
P577
1990-06-01T00:00:00Z