Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
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Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationPolymerization defects within human telomerase are distinct from telomerase RNA and TEP1 bindingHepatitis B virus replicationSequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B virusesSpecific incorporation of heat shock protein 70 family members into primate lentiviral virionsHepatitis B virus reverse transcriptase: diverse functions as classical and emerging targets for antiviral interventionCritical Role of Cyclophilin A and Its Prolyl-Peptidyl Isomerase Activity in the Structure and Function of the Hepatitis C Virus Replication ComplexTwo chaperone sites in Hsp90 differing in substrate specificity and ATP dependenceMolecular biology of hepatitis B virus infectionFunctional requirement of p23 and Hsp90 in telomerase complexesInhibition of heat-shock protein 90 reduces Ebola virus replicationThe cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activitySubstrate-binding characteristics of proteins in the 90 kDa heat shock protein familyCellular growth kinetics distinguish a cyclophilin inhibitor from an HSP90 inhibitor as a selective inhibitor of hepatitis C virusThe hepatitis B virus ribonuclease H is sensitive to inhibitors of the human immunodeficiency virus ribonuclease H and integrase enzymesGenome-wide and differential proteomic analysis of hepatitis B virus and aflatoxin B1 related hepatocellular carcinoma in Guangxi, ChinaHeat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infectionMolecular cloning of a novel chaperone-like protein induced by rhabdovirus infection with sequence similarity to the bacterial extracellular solute-binding protein family 5.SELEX-derived aptamers of the duck hepatitis B virus RNA encapsidation signal distinguish critical and non-critical residues for productive initiation of reverse transcription.Biological heterogeneity of the peptide-binding motif of the 70-kDa heat shock protein by surface plasmon resonance analysis.Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues.A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication.Effects of genomic length on translocation of hepatitis B virus polymerase-linked oligomer.Double-stranded linear duck hepatitis B virus (DHBV) stably integrates at a higher frequency than wild-type DHBV in LMH chicken hepatoma cells.Properties of monoclonal antibodies directed against hepatitis B virus polymerase protein.Mapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interactionBioactivities of Compounds from Elephantopus scaber, an Ethnomedicinal Plant from Southwest China.Expression of a viral polymerase-bound host factor turns human cell lines permissive to a plant- and insect-infecting virus.Functional characterization of naturally occurring variants of human hepatitis B virus containing the core internal deletion mutation.The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells.In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles.Human hepatitis B virus polymerase interacts with the molecular chaperonin Hsp60.Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coliHepatitis B virus biology.Reverse transcription-associated dephosphorylation of hepadnavirus nucleocapsids.Sequences in the terminal protein and reverse transcriptase domains of the hepatitis B virus polymerase contribute to RNA binding and encapsidationHepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.Interferon prevents formation of replication-competent hepatitis B virus RNA-containing nucleocapsids.Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase
P2860
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P2860
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@en
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@nl
type
label
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@en
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@nl
prefLabel
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@en
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@nl
P2860
P356
P1476
Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase.
@en
P2860
P304
P356
10.1073/PNAS.93.3.1060
P407
P577
1996-02-01T00:00:00Z