Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
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Ixodes scapularis and Ixodes ricinus tick cell lines respond to infection with tick-borne encephalitis virus: transcriptomic and proteomic analysisHeat shock protein and heat shock factor 1 expression and localization in vaccinia virus infected human monocyte derived macrophages.Stress Beyond Translation: Poxviruses and MoreIdentification of Cellular Proteome Modifications in Response to West Nile Virus InfectionPoxvirus tropismInhibition of heat-shock protein 90 reduces Ebola virus replicationThe master regulator of the cellular stress response (HSF1) is critical for orthopoxvirus infectionHeat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infectionHost and viral proteins in the virion of Kaposi's sarcoma-associated herpesvirus.Molecular cloning of a novel chaperone-like protein induced by rhabdovirus infection with sequence similarity to the bacterial extracellular solute-binding protein family 5.A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication.Multi-faceted proteomic characterization of host protein complement of Rift Valley fever virus virions and identification of specific heat shock proteins, including HSP90, as important viral host factorsThe cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells.Vaccinia virus proteome: identification of proteins in vaccinia virus intracellular mature virion particles.Active participation of cellular chaperone Hsp90 in regulating the function of rotavirus nonstructural protein 3 (NSP3).Temperature sensitive influenza A virus genome replication results from low thermal stability of polymerase-cRNA complexes.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.Redistribution of cyclophilin A to viral factories during vaccinia virus infection and its incorporation into mature particlesEvolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance.Heat-shock treatment-mediated increase in transduction by recombinant adeno-associated virus 2 vectors is independent of the cellular heat-shock protein 90Potential vaccines and post-exposure treatments for filovirus infections.Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro.Molecular chaperones in pathogen virulence: emerging new targets for therapy.Inhibition of HSP90 attenuates porcine reproductive and respiratory syndrome virus production in vitroRegulation of Viral Replication, Apoptosis and Pro-Inflammatory Responses by 17-AAG during Chikungunya Virus Infection in Macrophages.Broad action of Hsp90 as a host chaperone required for viral replication.Development of Vaccinia reporter viruses for rapid, high content analysis of viral function at all stages of gene expression.Continuous cell lines from the Muscovy duck as potential replacement for primary cells in the production of avian vaccines.A new post-PKS modification process in the carbamoyltransferase gene inactivation strain of Streptomyces hygroscopicus 17997.Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses.Protein Primary Structure of the Vaccinia Virion at Increased ResolutionIdentification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis.Survey of molecular chaperone requirement for the biosynthesis of hamster polyomavirus VP1 protein in Saccharomyces cerevisiae.Differential role played by the MEK/ERK/EGR-1 pathway in orthopoxviruses vaccinia and cowpox biology.Proteomic analysis of purified coronavirus infectious bronchitis virus particles.Geldanamycin, a potent and specific inhibitor of Hsp90, inhibits gene expression and replication of human cytomegalovirus.
P2860
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P2860
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
description
2002 nî lūn-bûn
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2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@ast
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@en
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@nl
type
label
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@ast
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@en
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@nl
prefLabel
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@ast
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@en
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@nl
P2093
P2860
P1433
P1476
Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
@en
P2093
Che-Sheng Chung
Jan-Jong Hung
P2860
P304
P356
10.1128/JVI.76.3.1379-1390.2002
P407
P577
2002-02-01T00:00:00Z