A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein.
about
Assessing the contribution of the herpes simplex virus DNA polymerase to spontaneous mutationsThe potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1Characterization of the chromosomal binding sites and dimerization partners of the viral oncoprotein Meq in Marek's disease virus-transformed T cellsOrigin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.Herpes simplex virus DNA packaging sequences adopt novel structures that are specifically recognized by a component of the cleavage and packaging machineryEvidence that the immediate-early gene product ICP4 is necessary for the genome of the herpes simplex virus type 1 ICP4 deletion mutant strain d120 to circularize in infected cellsComplementary intrastrand base pairing during initiation of Herpes simplex virus type 1 DNA replicationStructural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from herpes simplex virus type I.Sequence requirements for interaction of human herpesvirus 7 origin binding protein with the origin of lytic replication.Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.The linear plastid chromosomes of maize: terminal sequences, structures, and implications for DNA replication.Stepwise evolution of the herpes simplex virus origin binding protein and origin of replicationStructural polymorphism exhibited by a quasipalindrome present in the locus control region (LCR) of the human beta-globin gene cluster.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.Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.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.Activation of the herpes simplex virus type-1 origin-binding protein (UL9) by heat shock proteins.
P2860
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P2860
A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
A novel conformation of the he ...... by the origin binding protein.
@en
type
label
A novel conformation of the he ...... by the origin binding protein.
@en
prefLabel
A novel conformation of the he ...... by the origin binding protein.
@en
P2093
P2860
P356
P1476
A novel conformation of the he ...... by the origin binding protein.
@en
P2093
P2860
P304
P356
10.1074/JBC.275.8.5880
P407
P577
2000-02-01T00:00:00Z