Partial functional complementation of a pseudorabies virus UL25 deletion mutant by herpes simplex virus type 1 pUL25 indicates overlapping functions of alphaherpesvirus pUL25 proteins.
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A "coiled-coil" motif is important for oligomerization and DNA binding properties of human cytomegalovirus protein UL77Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Uncoupling uncoating of herpes simplex virus genomes from their nuclear import and gene expression.The C Terminus of the Herpes Simplex Virus UL25 Protein Is Required for Release of Viral Genomes from Capsids Bound to Nuclear Pores.Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins.Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsidsThe way out: what we know and do not know about herpesvirus nuclear egress.A physical link between the pseudorabies virus capsid and the nuclear egress complex.Mapping of sequences in Pseudorabies virus pUL34 that are required for formation and function of the nuclear egress complex.Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53.Human Cytomegalovirus pUL93 Links Nucleocapsid Maturation and Nuclear Egress.Mutational analysis of the herpes simplex virus type 1 UL25 DNA packaging protein reveals regions that are important after the viral DNA has been packaged.The UL25 gene product of herpes simplex virus type 1 is involved in uncoating of the viral genomeCharacterization of pseudorabies virus (PrV) cleavage-encapsidation proteins and functional complementation of PrV pUL32 by the homologous protein of herpes simplex virus type 1.The Essential Human Cytomegalovirus Proteins pUL77 and pUL93 Are Structural Components Necessary for Viral Genome Encapsidation.Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1Herpesvirus Nuclear Egress.Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25.Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation.A pUL25 dimer interfaces the pseudorabies virus capsid and tegument.Venture from the Interior-Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane.
P2860
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P2860
Partial functional complementation of a pseudorabies virus UL25 deletion mutant by herpes simplex virus type 1 pUL25 indicates overlapping functions of alphaherpesvirus pUL25 proteins.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Partial functional complementa ...... phaherpesvirus pUL25 proteins.
@en
type
label
Partial functional complementa ...... phaherpesvirus pUL25 proteins.
@en
prefLabel
Partial functional complementa ...... phaherpesvirus pUL25 proteins.
@en
P2093
P2860
P356
P1433
P1476
Partial functional complementa ...... phaherpesvirus pUL25 proteins.
@en
P2093
Barbara G Klupp
Harald Granzow
Tobias Leege
Walter Fuchs
P2860
P304
P356
10.1128/JVI.02441-07
P407
P577
2008-04-09T00:00:00Z