The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.
about
Hepatitis B virus polymerase blocks pattern recognition receptor signaling via interaction with DDX3: implications for immune evasionIdentification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptaseCombining genetic and biochemical approaches to identify functional molecular contact points.RNA elements directing translation of the duck hepatitis B Virus polymerase via ribosomal shunting.Cryptic protein priming sites in two different domains of duck hepatitis B virus reverse transcriptase for initiating DNA synthesis in vitro.Extensive mutagenesis of the conserved box E motif in duck hepatitis B virus P protein reveals multiple functions in replication and a common structure with the primer grip in HIV-1 reverse transcriptaseProtein-primed terminal transferase activity of hepatitis B virus polymerase.Intracellular transport of hepatitis B virus.Pre-P is a secreted glycoprotein encoded as an N-terminal extension of the duck hepatitis B virus polymerase gene.Hepatitis B Virus Polymerase Localizes to the Mitochondria, and Its Terminal Protein Domain Contains the Mitochondrial Targeting Signal.Nuclear Import of Hepatitis B Virus Capsids and Genome.Exposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173).Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation.Purification and enzymatic characterization of the hepatitis B virus ribonuclease H, a new target for antiviral inhibitors.DDX3 DEAD-Box RNA helicase inhibits hepatitis B virus reverse transcription by incorporation into nucleocapsids.The C terminus of foamy retrovirus Gag contains determinants for encapsidation of Pol protein into virions.Translation of duck hepatitis B virus reverse transcriptase by ribosomal shunting.The duck hepatitis B virus reverse transcriptase functions as a full-length monomer.Role of p50/CDC37 in hepadnavirus assembly and replication.Identification and characterization of a novel bipartite nuclear localization signal in the hepatitis B virus polymeraseKinetics of synthesis and turnover of the duck hepatitis B virus reverse transcriptase.
P2860
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P2860
The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.
description
2000 nî lūn-bûn
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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@ast
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@en
type
label
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@ast
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@en
prefLabel
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@ast
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@en
P2093
P2860
P1433
P1476
The majority of duck hepatitis ...... nd to a cytoplasmic structure.
@en
P2093
P2860
P304
P356
10.1128/JVI.74.18.8648-8657.2000
P577
2000-09-01T00:00:00Z