ArticleJournal of virology2000
The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Preparation and functional evaluation of monoclonal antibodies targeting Hepatitis B Virus Polymerase.Virulence · 2021Article
- Nuclear Import of Hepatitis B Virus Capsids and Genome.Viruses · 2017Review
- Hepatitis B Virus Polymerase Localizes to the Mitochondria, and Its Terminal Protein Domain Contains the Mitochondrial Targeting Signal.Journal of virology · 2016Article
- Purification and enzymatic characterization of the hepatitis B virus ribonuclease H, a new target for antiviral inhibitors.Antiviral research · 2016Article
- Identification and characterization of a novel bipartite nuclear localization signal in the hepatitis B virus polymerase.World journal of gastroenterology · 2013Article
- Protein-primed terminal transferase activity of hepatitis B virus polymerase.Journal of virology · 2013Article
- 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 transcriptase.Journal of virology · 2012Article
- Cryptic protein priming sites in two different domains of duck hepatitis B virus reverse transcriptase for initiating DNA synthesis in vitro.Journal of virology · 2011Article
- RNA elements directing translation of the duck hepatitis B Virus polymerase via ribosomal shunting.Journal of virology · 2011Article
- Hepatitis B virus polymerase blocks pattern recognition receptor signaling via interaction with DDX3: implications for immune evasion.PLoS pathogens · 2010Article
- DDX3 DEAD-Box RNA helicase inhibits hepatitis B virus reverse transcription by incorporation into nucleocapsids.Journal of virology · 2009Article
- Pre-P is a secreted glycoprotein encoded as an N-terminal extension of the duck hepatitis B virus polymerase gene.Journal of virology · 2009Article
- The C terminus of foamy retrovirus Gag contains determinants for encapsidation of Pol protein into virions.Journal of virology · 2008Article
- Intracellular transport of hepatitis B virus.World journal of gastroenterology · 2007Review
- Combining genetic and biochemical approaches to identify functional molecular contact points.Biological procedures online · 2006Article
- Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase.Journal of virology · 2005Article
- 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).Journal of virology · 2005Article
- Translation of duck hepatitis B virus reverse transcriptase by ribosomal shunting.Journal of virology · 2004Article
- Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation.Journal of virology · 2001Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The hepadnavirus reverse transcriptase binds cotranslationally to the viral pregenomic RNA. This ribonucleoprotein complex is then encapsidated into nascent viral core particles, where the reverse transcriptase copies the viral RNA into DNA. Here we report that 75% of the duck hepatitis B virus reverse transcriptase present in transfected LMH cells does not follow this well-known pathway but rather exists in the cell separate from the core protein or nucleocapsids. The nonencapsidated reverse transcriptase is also abundant in infected duck liver. The nonencapsidated reverse transcriptase exists as a complex set of isoforms that are most likely produced by posttranslational modification. Interestingly, only the smallest of these isoforms is encapsidated into viral core particles. The nonencapsidated reverse transcriptase is bound to a large cellular cytoplasmic structure(s) in a detergent-sensitive complex. The cellular distribution of the reverse transcriptase only partially overlaps that of the core protein, and this distribution is unaffected by blocking encapsidation. These observations raise the possibilities that the metabolic fate of the reverse transcriptase may be posttranscriptionally regulated and that the reverse transcriptase may have roles in the viral replication cycle beyond its well-known function in copying the viral genome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.