Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection
about
USP11 stabilizes HPV-16E7 and further modulates the E7 biological activityProteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleusVisualization of the herpes simplex virus portal in situ by cryo-electron tomographyAlpha-herpesvirus infection induces the formation of nuclear actin filamentsSCaMC-1Like a member of the mitochondrial carrier (MC) family preferentially expressed in testis and localized in mitochondria and chromatoid bodyCyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinasesIdentification of Viral and Host Proteins That Interact with Murine Gammaherpesvirus 68 Latency-Associated Nuclear Antigen during Lytic Replication: a Role for Hsc70 in Viral ReplicationHeat-shock protein 90 promotes nuclear transport of herpes simplex virus 1 capsid protein by interacting with acetylated tubulinHsp70 Isoforms Are Essential for the Formation of Kaposi's Sarcoma-Associated Herpesvirus Replication and Transcription CompartmentsSpatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click ChemistryDisulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Herpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.Relocalization of upstream binding factor to viral replication compartments is UL24 independent and follows the onset of herpes simplex virus 1 DNA synthesisHost and viral proteins in the virion of Kaposi's sarcoma-associated herpesvirus.Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infectionICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Bortezomib-induced unfolded protein response increases oncolytic HSV-1 replication resulting in synergistic antitumor effects.Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/NXF1.The cellular localization pattern of Varicella-Zoster virus ORF29p is influenced by proteasome-mediated degradationComposition of pseudorabies virus particles lacking tegument protein US3, UL47, or UL49 or envelope glycoprotein E.A Hsp40 chaperone protein interacts with and modulates the cellular distribution of the primase protein of human cytomegalovirus.A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virusHeat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway.Accumulation of oxidized proteins in Herpesvirus infected cells.Baculovirus IE2 Stimulates the Expression of Heat Shock Proteins in Insect and Mammalian Cells to Facilitate Its Proper Functioning.An siRNA Screen Identifies the U2 snRNP Spliceosome as a Host Restriction Factor for Recombinant Adeno-associated VirusesHepatitis E virus replication requires an active ubiquitin-proteasome system.Herpes simplex virus 1 VP22 regulates translocation of multiple viral and cellular proteins and promotes neurovirulence.Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: Potential role in blocking IFN-beta induction.Innate recognition network driving herpes simplex virus-induced corneal immunopathology: role of the toll pathway in early inflammatory events in stromal keratitisCellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step.Domain within herpes simplex virus 1 scaffold proteins required for interaction with portal protein in infected cells and incorporation of the portal vertex into capsids.Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.Nuclear pore composition and gating in herpes simplex virus-infected cellsThe co-chaperone BAG3 regulates Herpes Simplex Virus replication.
P2860
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P2860
Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection
description
2004 nî lūn-bûn
@nan
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@ast
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@en
type
label
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@ast
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@en
prefLabel
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@ast
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@en
P2860
P1433
P1476
Nuclear sequestration of cellu ...... simplex virus type 1 infection
@en
P2093
April D Burch
P2860
P304
P356
10.1128/JVI.78.13.7175-7185.2004
P577
2004-07-01T00:00:00Z