ArticleJournal of virology2009
Ubiquitin-independent degradation of hepatitis C virus F protein.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 56 citations in OpenAlex.
- Human Viral Oncoproteins and Ubiquitin-Proteasome System.Global medical genetics · 2024Review
- Hepatitis C virus induces oxidation and degradation of apolipoprotein B to enhance lipid accumulation and promote viral production.PLoS pathogens · 2021Article
- Genotypic Regulation of Type I Interferon Induction Pathways by Frameshift (F) Proteins of Hepatitis C Virus.Journal of virology · 2020Article
- Detection of active proteasome structures in brain extracts: proteasome features of August rat brain with violations in monoamine metabolism.Oncotarget · 2017Article
- Native structure of rat liver immune proteasomes.Doklady. Biochemistry and biophysics · 2016Article
- Two Degradation Pathways of the p35 Cdk5 (Cyclin-dependent Kinase) Activation Subunit, Dependent and Independent of Ubiquitination.The Journal of biological chemistry · 2016Article
- Chaperones in hepatitis C virus infection.World journal of hepatology · 2016Review
- Article
- Inhibition of hepatitis E virus replication by proteasome inhibitor is nonspecific.Archives of virology · 2015Article
- Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation.Biomolecules · 2014Review
- Production and pathogenicity of hepatitis C virus core gene products.World journal of gastroenterology · 2014Review
- PA28αβ: the enigmatic magic ring of the proteasome?Biomolecules · 2014Review
- The ubiquitin-proteasome system in positive-strand RNA virus infection.Reviews in medical virology · 2013Review
- Roles of the two distinct proteasome pathways in hepatitis C virus infection.World journal of virology · 2012Article
- The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits.Biochemical and biophysical research communications · 2012Article
- Ubiquitin-independent proteasomal degradation during oncogenic viral infections.Biochimica et biophysica acta · 2011Review
- Simplified RNA secondary structure mapping by automation of SHAPE data analysis.Nucleic acids research · 2011Article
- Cooperation between an intrinsically disordered region and a helical segment is required for ubiquitin-independent degradation by the proteasome.The Journal of biological chemistry · 2011Article
- Identification of immunogenic regions within the alternative reading frame protein of hepatitis C virus (genotype 3).European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2011Article
- Synonymous mutations in the core gene are linked to unusual serological profile in hepatitis C virus infection.PloS one · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Hepatitis C virus (HCV) F protein is encoded by the +1 reading frame of the viral genome. It overlaps with the core protein coding sequence, and multiple mechanisms for its expression have been proposed. The full-length F protein that is synthesized by translational ribosomal frameshift at codons 9 to 11 of the core protein sequence is a labile protein. By using a combination of genetic, biochemical, and cell biological approaches, we demonstrate that this HCV F protein can bind to the proteasome subunit protein alpha3, which reduces the F-protein level in cells in a dose-dependent manner. Deletion-mapping analysis identified amino acids 40 to 60 of the F protein as the alpha3-binding domain. This alpha3-binding domain of the F protein together with its upstream sequence could significantly destabilize the green fluorescent protein, an otherwise stable protein. Further analyses using an F-protein mutant lacking lysine and a cell line that contained a temperature-sensitive E1 ubiquitin-activating enzyme indicated that the degradation of the F protein was ubiquitin independent. Based on these observations as well as the observation that the F protein could be degraded directly by the 20S proteasome in vitro, we propose that the full-length HCV F protein as well as the F protein initiating from codon 26 is degraded by an ubiquitin-independent pathway that is mediated by the proteasome subunit alpha3. The ability of the F protein to bind to alpha3 raises the possibility that the HCV F protein may regulate protein degradation in cells.
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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.