A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.
about
An integrated approach to elucidate the intra-viral and viral-cellular protein interaction networks of a gamma-herpesvirusIdentification of delta helicase as the bovine homolog of HUPF1: demonstration of an interaction with the third subunit of DNA polymerase delta.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 alphaOrigin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new membersThe DNA helicase-primase complex as a target for herpes viral infectionThe Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication.Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex.Molecular dissection of the domain architecture and catalytic activities of human PrimPol.Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationRecruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Baculovirus late expression factors.A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.Understanding helicases as a means of virus control.Replication and recombination of herpes simplex virus DNAThe UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding.Coordinated leading and lagging strand DNA synthesis by using the herpes simplex virus 1 replication complex and minicircle DNA templatesHerpes simplex virus-1 helicase-primase: roles of each subunit in DNA binding and phosphodiester bond formation.PrimPol-Prime Time to Reprime.UL52 primase interactions in the herpes simplex virus 1 helicase-primase are affected by antiviral compounds and mutations causing drug resistanceDepletion of intracellular zinc inhibits the ubiquitin ligase activity of viral regulatory protein ICP0 and restricts herpes simplex virus 1 replication in cell culture.A complex zinc finger controls the enzymatic activities of nidovirus helicasesEpstein-barr virus encodes three bona fide ubiquitin-specific proteases.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Cysteine 111 affects coupling of single-stranded DNA binding to ATP hydrolysis in the herpes simplex virus type-1 origin-binding protein.Identification of Amino Acids Essential for Viral Replication in the HCMV Helicase-Primase Complex
P2860
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P2860
A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
A mutation in the C-terminal p ...... 1 helicase-primase subcomplex.
@en
type
label
A mutation in the C-terminal p ...... 1 helicase-primase subcomplex.
@en
prefLabel
A mutation in the C-terminal p ...... 1 helicase-primase subcomplex.
@en
P2860
P356
P1476
A mutation in the C-terminal p ...... -1 helicase-primase subcomplex
@en
P2093
P2860
P304
P356
10.1074/JBC.274.12.8068
P407
P577
1999-03-01T00:00:00Z