Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation. - Wikidata - wikimedia - TriplyDB

Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.

Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.

http://www.wikidata.org/entity/Q36747965

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The DNA helicase-primase complex as a target for herpes viral infection Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.Spatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click Chemistry The HSV-1 exonuclease, UL12, stimulates recombination by a single strand annealing mechanism Herpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled.Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.Hsp90 and Hsp40/Erdj3 are required for the expression and anti-apoptotic function of KSHV K1 Structure of the herpes simplex virus 1 genome: manipulation of nicks and gaps can abrogate infectivity and alter the cellular DNA damage response.Efficient herpes simplex virus 1 replication requires cellular ATR pathway proteins Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.Inhibition of HSP70 reduces porcine reproductive and respiratory syndrome virus replication in vitro.Accumulation of oxidized proteins in Herpesvirus infected cells.DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication Herpes simplex virus 1 VP22 regulates translocation of multiple viral and cellular proteins and promotes neurovirulence.Herpes simplex viruses: mechanisms of DNA replication.The co-chaperone BAG3 regulates Herpes Simplex Virus replication.Replication and recombination of herpes simplex virus DNA DNA virus replication compartments.An Intrinsically Disordered Region of the DNA Repair Protein Nbs1 Is a Species-Specific Barrier to Herpes Simplex Virus 1 in Primates.Genetic Confirmation that the H5 Protein Is Required for Vaccinia Virus DNA Replication.Requirement of the N-terminal activation domain of herpes simplex virus ICP4 for viral gene expression.ICP8 Filament Formation Is Essential for Replication Compartment Formation during Herpes Simplex Virus Infection Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.Proteasome subunits relocalize during human cytomegalovirus infection, and proteasome activity is necessary for efficient viral gene transcription.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.PNKP knockdown by RNA interference inhibits herpes simplex virus-1 replication in astrocytes.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.The replication cycle of varicella-zoster virus: analysis of the kinetics of viral protein expression, genome synthesis, and virion assembly at the single-cell level.Small interfering RNA targeting for infected-cell polypeptide 4 inhibits herpes simplex virus type 1 replication in retinal pigment epithelial cells.

P2860

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P2860

Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.

http://www.wikidata.org/entity/Q36747965

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Oligomerization of ICP4 and re ...... prereplicative site formation.

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type

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Oligomerization of ICP4 and re ...... prereplicative site formation.

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Oligomerization of ICP4 and re ...... prereplicative site formation.

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P1433

Journal of Virology

P1476

Oligomerization of ICP4 and re ...... prereplicative site formation.

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P2093

Christine M Livingston

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Dianna E Wilkinson

http://www.w3.org/2001/XMLSchema#string

Neal A DeLuca

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Sandra K Weller

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P2860

PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0

Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes

PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1

Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies

Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection

ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection.

Nuclear aggresomes form by fusion of PML-associated aggregates.

Stability and nuclear distribution of mammalian replication protein A heterotrimeric complex.

Proteasome-dependent processing of nuclear proteins is correlated with their subnuclear localization.

Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies.

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6324-6336

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scholarly article

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10.1128/JVI.00455-08

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13

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82

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2447070

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