Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.
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The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNAMany ways to loop DNA.The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping.Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseRole of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationThe Kaposi's sarcoma-associated herpesvirus ORF6 DNA binding protein forms long DNA-free helical protein filamentsReconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1Herpes simplex viruses: mechanisms of DNA replication.Understanding helicases as a means of virus control.Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: involvement of host cellular factorsFunctional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activityStructural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.Replication and recombination of herpes simplex virus DNATargeting Holliday junctions by origin DNA-binding protein of herpes simplex virus type 1.Role of protein-protein interactions during herpes simplex virus type 1 recombination-dependent replication.Human cytomegalovirus UL84 oligomerization and heterodimerization domains act as transdominant inhibitors of oriLyt-dependent DNA replication: evidence that IE2-UL84 and UL84-UL84 interactions are required for lytic DNA replicationInitiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Stepwise evolution of the herpes simplex virus origin binding protein and origin of replicationEvidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.Interaction of Kaposi's sarcoma-associated herpesvirus ORF59 with oriLyt is dependent on binding with K-Rta.Functional properties of the herpes simplex virus type I origin-binding protein are controlled by precise interactions with the activated form of the origin of DNA replication.
P2860
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P2860
Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Origin-specific unwinding of h ...... specific preunwinding complex.
@ast
Origin-specific unwinding of h ...... specific preunwinding complex.
@en
Origin-specific unwinding of h ...... specific preunwinding complex.
@nl
type
label
Origin-specific unwinding of h ...... specific preunwinding complex.
@ast
Origin-specific unwinding of h ...... specific preunwinding complex.
@en
Origin-specific unwinding of h ...... specific preunwinding complex.
@nl
prefLabel
Origin-specific unwinding of h ...... specific preunwinding complex.
@ast
Origin-specific unwinding of h ...... specific preunwinding complex.
@en
Origin-specific unwinding of h ...... specific preunwinding complex.
@nl
P2093
P2860
P356
P1476
Origin-specific unwinding of h ...... specific preunwinding complex.
@en
P2093
Alexander M Makhov
I Robert Lehman
Jack D Griffith
Sam S-K Lee
P2860
P304
P356
10.1073/PNAS.0237171100
P407
P577
2003-01-24T00:00:00Z