The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells.
about
Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationHepatitis B virus replicationViruses and antiviral immunity in DrosophilaThree-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelleMechanisms of genetic robustness in RNA virusesDevelopment of Sindbis Viruses Encoding nsP2/GFP Chimeric Proteins and Their Application for Studying nsP2 FunctioningIdentification of Cellular Proteome Modifications in Response to West Nile Virus InfectionCochaperone Activity of Human Butyrate-Induced Transcript 1 Facilitates Hepatitis C Virus Replication through an Hsp90-Dependent PathwayInhibition of heat-shock protein 90 reduces Ebola virus replicationCritical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNAA key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes.Complementary transcriptomic, lipidomic, and targeted functional genetic analyses in cultured Drosophila cells highlight the role of glycerophospholipid metabolism in Flock House virus RNA replicationA targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication.Proteomic analysis of primary duck hepatocytes infected with duck hepatitis B virusThe hop-like stress-induced protein 1 cochaperone is a novel cell-intrinsic restriction factor for mitochondrial tombusvirus replication.The dependence of viral RNA replication on co-opted host factors.Hsp90 interacts specifically with viral RNA and differentially regulates replication initiation of Bamboo mosaic virus and associated satellite RNAThe C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial complex I subunit.Membrane-bound tomato mosaic virus replication proteins participate in RNA synthesis and are associated with host proteins in a pattern distinct from those that are not membrane bound.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.Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance.A functional heat shock protein 90 chaperone is essential for efficient flock house virus RNA polymerase synthesis in Drosophila cells.Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection.The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiaeRecent insights into the biology and biomedical applications of Flock House virusIn vitro assembly of the Tomato bushy stunt virus replicase requires the host Heat shock protein 70Mitochondrion-enriched anionic phospholipids facilitate flock house virus RNA polymerase membrane association.Characterization of a nodavirus replicase revealed a de novo initiation mechanism of RNA synthesis and terminal nucleotidyltransferase activityRole of cellular lipids in positive-sense RNA virus replication complex assembly and function.Broad action of Hsp90 as a host chaperone required for viral replication.The role of mutational robustness in RNA virus evolution.Restriction of rift valley Fever virus virulence in mosquito cells.Maturation-dependent responses of human neuronal cells to western equine encephalitis virus infection and type I interferons.Virus and dsRNA-triggered transcriptional responses reveal key components of honey bee antiviral defense.Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses.A furoviral replicase recruits host HSP70 to membranes for viral RNA replication.Flock house virus RNA polymerase initiates RNA synthesis de novo and possesses a terminal nucleotidyl transferase activity.A temperature sensitive mutant of heat shock protein 70 reveals an essential role during the early steps of tombusvirus replication.Proteomic analysis of purified coronavirus infectious bronchitis virus particles.
P2860
Q24305040-BF20E129-2ED7-41A5-A4B8-000F393E177FQ24563894-0A163AAB-04B0-4CEE-B409-212DC701B7DFQ26998819-C2611ACC-9533-4CDF-AA8D-03F1236F7721Q27334421-23A56272-0674-4063-8AF0-3F9A264D29DFQ27472944-84DE0D9D-8AA8-473C-BB27-7D16CB560DB4Q27480350-2C37A3F3-6DF0-4289-BBDF-7CEC65875AC9Q27488891-8ED401BD-967D-483F-ADAB-5AF4B5C29DA7Q27489790-2B1077B6-3970-4BAC-91C3-A32E755F5E54Q28281834-A9DDE2A5-767E-4560-A387-308D94B0E389Q28504793-199E4BA8-E2A8-4220-8A7D-C06F25B11DD8Q33400948-7923698B-C49F-425D-8739-B79A23321092Q33541729-AD7F3256-A73B-424A-8B90-5078D4219419Q33558724-6B9970B6-AB7D-47F6-ABF9-7983924C9913Q33997952-18F380B5-723E-409B-98F4-2E9981127F48Q34059324-0314C96C-B928-4BAB-8057-6B764305B58BQ34241671-4BAA9C82-6320-40BE-B2F0-69118C1B4960Q34288791-B5C9FAA2-41AD-429D-9D3A-32189C5763F4Q34333891-DE96D96D-954F-48AB-929C-31E03876C24CQ35024089-DCDD4E7E-767E-42EB-927C-061DBC483772Q35164980-DC31CE54-6BBB-473E-B888-F7418AEDE330Q35169647-CD0E3B8E-C6DA-491B-A04D-482494850D27Q35589164-973762B8-A9C7-46F6-91D4-2BF4D7E6ED55Q35947748-003856D9-7D5D-49E0-9C9C-9690330A9626Q36449775-DC824B50-7FD2-4A12-BF7D-BEDCE475FA52Q36483294-365AFD58-D20C-49C6-B4F6-8D7C6EFE1249Q36877226-2D31569D-7B7C-44C0-BC2D-4D42314317C4Q37018802-2EC1A1D5-830F-4C38-9810-E9B9696184E3Q37157148-155B373A-2C40-41C9-8296-B1A0D99D354DQ37312097-124AB766-8500-4FEB-9618-650E2D320386Q37945204-F22F8B33-32C8-4C96-98E9-72B5DA04D10CQ37966479-2D8AF882-349D-4DCF-9F61-69E3B7724E18Q38092577-D9D5DA07-E6BB-46DB-89B8-C16F5BCF9912Q38614407-B9A4C065-FB7C-4063-8E38-A6FB79D0C411Q40049486-8636041D-8FDE-4A30-B982-77AC2BA95D98Q40108593-781C9867-CCE8-4A10-A6B0-0EEB3E4E6D61Q40178192-E3935BE4-DF58-4206-98E2-DBC33E528C41Q40262622-01AF4BD8-63AB-4D1E-851F-8596606AEE24Q41888697-CDB40ECA-A140-4B0F-AEF9-7D781C41F5C0Q42188683-FF38FA44-147A-4013-9EBE-39E0E53CC15FQ42702837-9578B24C-0FAA-4700-A6B7-358B20ED92E2
P2860
The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
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
name
The cellular chaperone heat sh ...... plication in Drosophila cells.
@ast
The cellular chaperone heat sh ...... plication in Drosophila cells.
@en
type
label
The cellular chaperone heat sh ...... plication in Drosophila cells.
@ast
The cellular chaperone heat sh ...... plication in Drosophila cells.
@en
prefLabel
The cellular chaperone heat sh ...... plication in Drosophila cells.
@ast
The cellular chaperone heat sh ...... plication in Drosophila cells.
@en
P2860
P1433
P1476
The cellular chaperone heat sh ...... plication in Drosophila cells.
@en
P2093
David J Miller
Kathryn M Kampmueller
P2860
P304
P356
10.1128/JVI.79.11.6827-6837.2005
P577
2005-06-01T00:00:00Z