Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding.
about
Unraveling DNA helicases. Motif, structure, mechanism and functionIGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1)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 alphaIntersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spotsThe DNA helicase-primase complex as a target for herpes viral infectionHelicase and capping enzyme active site mutations in brome mosaic virus protein 1a cause defects in template recruitment, negative-strand RNA synthesis, and viral RNA capping.Dna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growthHelicase motifs: the engine that powers DNA unwinding.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.An intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity.Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9.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.Oral bioavailability and in vivo efficacy of the helicase-primase inhibitor BILS 45 BS against acyclovir-resistant herpes simplex virus type 1.HSV-1 protein expression using recombinant baculovirusesA 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.Herpes simplex viruses: mechanisms of DNA replication.Understanding helicases as a means of virus control.Helicases as prospective targets for anti-cancer therapy.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.A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.A kinetic analysis of the oligonucleotide-modulated ATPase activity of the helicase domain of the NS3 protein from hepatitis C virus. The first cycle of interaction of ATP with the enzyme is unique.Herpes simplex virus-1 helicase-primase: roles of each subunit in DNA binding and phosphodiester bond formation.HSV-I and the cellular DNA damage response.A region near the C-terminal end of Escherichia coli DNA helicase II is required for single-stranded DNA bindingDrosophila melanogaster RECQ5/QE DNA helicase: stimulation by GTP binding.Conserved motifs II to VI of DNA helicase II from Escherichia coli are all required for biological activity.Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: only a subset are likely to be precursors to replication compartments.A single SNP, G929T (Gly310Val), determines the presence of a functional and a non-functional allele of HIS4 in Candida albicans SC5314: detection of the non-functional allele in laboratory strains.The primary and secondary translocase activities within E. coli RecBC helicase are tightly coupled to ATP hydrolysis by the RecB motorResidues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.Structure and Mechanisms of SF1 DNA Helicases.ASP2151, a novel helicase-primase inhibitor, possesses antiviral activity against varicella-zoster virus and herpes simplex virus types 1 and 2.Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae.Chikungunya virus nsP1 interacts directly with nsP2 and modulates its ATPase activity.The ENU-induced cetus mutation reveals an essential role of the DNA helicase DDX11 for mesoderm development during early mouse embryogenesis.
P2860
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P2860
Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Biochemical analyses of mutati ...... ween hydrolysis and unwinding.
@en
type
label
Biochemical analyses of mutati ...... ween hydrolysis and unwinding.
@en
prefLabel
Biochemical analyses of mutati ...... ween hydrolysis and unwinding.
@en
P2093
P2860
P356
P1476
Biochemical analyses of mutati ...... ween hydrolysis and unwinding.
@en
P2093
Challberg MD
Gottlieb J
Graves-Woodward KL
P2860
P304
P356
10.1074/JBC.272.7.4623
P407
P577
1997-02-01T00:00:00Z