Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus.
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Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationHepatitis B virus replicationCritical Role of Cyclophilin A and Its Prolyl-Peptidyl Isomerase Activity in the Structure and Function of the Hepatitis C Virus Replication ComplexInhibition of heat-shock protein 90 reduces Ebola virus replicationCyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinasesHsp90 inhibitors are efficacious against Kaposi Sarcoma by enhancing the degradation of the essential viral gene LANA, of the viral co-receptor EphA2 as well as other client proteinsHeat-shock protein 90 promotes nuclear transport of herpes simplex virus 1 capsid protein by interacting with acetylated tubulinHeat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infectionHsp70 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 ChemistryHerpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complexHsc70 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 infectionA targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication.Temperature protects insect cells from infection by cricket paralysis virus.Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism.Hsp90 and Hsp40/Erdj3 are required for the expression and anti-apoptotic function of KSHV K1Bortezomib-induced unfolded protein response increases oncolytic HSV-1 replication resulting in synergistic antitumor effects.A Hsp40 chaperone protein interacts with and modulates the cellular distribution of the primase protein of human cytomegalovirus.Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin.High-throughput screen of natural product libraries for hsp90 inhibitors.Extracellular Hsp90 serves as a co-factor for MAPK activation and latent viral gene expression during de novo infection by KSHV.Accumulation of oxidized proteins in Herpesvirus infected cells.Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance.A Panel of Stably Expressed Reference Genes for Real-Time qPCR Gene Expression Studies of Mallards (Anas platyrhynchos).Herpes simplex viruses: mechanisms of DNA replication.Analysis of protein expression profiles in the thymus of chickens infected with Marek's disease virus.The Pseudorabies Virus DNA Polymerase Accessory Subunit UL42 Directs Nuclear Transport of the Holoenzyme.Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.Transcriptional and Bioinformatic Analysis Provide a Relationship between Host Response Changes to Marek's Disease Viruses Infection and an Integrated Long Terminal Repeat.Functional Regulation of an Autographa californica Nucleopolyhedrovirus-Encoded MicroRNA, AcMNPV-miR-1, in Baculovirus Replication.Hsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cellsRegulated transport into the nucleus of herpesviridae DNA replication core proteins.HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replicationHerpes simplex virus 1 ICP22 but not US 1.5 is required for efficient acute replication in mice and VICE domain formation.Broad action of Hsp90 as a host chaperone required for viral replication.HSV-1 ICP22: hijacking host nuclear functions to enhance viral infection.DNA virus replication compartments.
P2860
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P2860
Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@en
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@nl
type
label
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@en
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@nl
prefLabel
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@en
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@nl
P2860
P1433
P1476
Herpes simplex virus type 1 DN ...... r localization to the nucleus.
@en
P2093
April D Burch
P2860
P304
10740-10749
P356
10.1128/JVI.79.16.10740-10749.2005
P407
P577
2005-08-01T00:00:00Z