Expression of herpes simplex virus type 1 DNA polymerase in Saccharomyces cerevisiae and detection of virus-specific enzyme activity in cell-free lysates
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Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulationCloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinaseMolecular cloning of mevalonate kinase and regulation of its mRNA levels in rat liverCharacterization of the DNA polymerase gene of human herpesvirus 6The multifunctional protein OBF1 is phosphorylated at serine and threonine residues in Saccharomyces cerevisiae.Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.Herpes simplex virus virion host shutoff protein requires a mammalian factor for efficient in vitro endoribonuclease activity.Resistance of herpesviruses to antiviral drugsEnzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells.Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction.Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateTwo regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype.Structure-function studies of the herpes simplex virus type 1 DNA polymerase.The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.Translational regulation of herpes simplex virus DNA polymerase.The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymeraseMutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.In vitro mutagenesis of the herpes simplex virus type 1 DNA polymerase gene results in altered drug sensitivity of the enzyme.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.
P2860
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P2860
Expression of herpes simplex virus type 1 DNA polymerase in Saccharomyces cerevisiae and detection of virus-specific enzyme activity in cell-free lysates
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Expression of herpes simplex v ...... activity in cell-free lysates
@en
type
label
Expression of herpes simplex v ...... activity in cell-free lysates
@en
prefLabel
Expression of herpes simplex v ...... activity in cell-free lysates
@en
P2093
P2860
P1433
P1476
Expression of herpes simplex v ...... activity in cell-free lysates
@en
P2093
C S Crumpacker
D I Dorsky
J T Stevens
M L Haffey
S M Wietstock
W T Ruyechan
P2860
P304
P407
P577
1988-12-01T00:00:00Z