ArticleAnalytical biochemistry2007
A method for in vitro assembly of hepatitis C virus core protein and for screening of inhibitors.
Article in Analytical biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Virus-like Particles as Vaccines for Allergen-Specific Therapy: An Overview of Current Developments.International journal of molecular sciences · 2024Review
- Comparison, Analysis, and Molecular Dynamics Simulations of Structures of a Viral Protein Modeled Using Various Computational Tools.Bioengineering (Basel, Switzerland) · 2023Article
- Identification of novel RNA secondary structures within the hepatitis C virus genome reveals a cooperative involvement in genome packaging.Scientific reports · 2016Article
- Article
- HCV core protein and virus assembly: what we know without structures.Immunologic research · 2014Review
- The hepatitis C virus core protein can modulate RNA-dependent RNA synthesis by the 2a polymerase.Virus research · 2014Article
- HCV core residues critical for infectivity are also involved in core-NS5A complex formation.PloS one · 2014Article
- Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.Journal of virology · 2010Article
- Core as a novel viral target for hepatitis C drugs.Viruses · 2010Article
- In vitro methods for testing antiviral drugs.Biotechnology advancesReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of hepatitis C virus (HCV) is not well understood. We investigated HCV nucleocapsid assembly in vitro and the role of electrostatic/hydrophobic interactions in this process. We developed a simple and rapid in vitro assay in which the progress of assembly is monitored by measuring an increase in turbidity, thereby allowing the kinetics of assembly to be determined. Assembly is performed using a truncated HCV core (C1-82), containing the minimal assembly domain, purified from Escherichia coli. The increase in turbidity is linked to the formation of nucleocapsid-like particles (NLPs) in solution, and nucleic acids are essential to initiate nucleocapsid assembly under the experimental conditions used. The sensitivity of NLP formation to salt strongly suggests that electrostatic forces govern in vitro assembly. Mutational analysis of C1-82 demonstrated that it is the global positive charge of C1-82 rather than any specific basic residue that is important for the assembly process. Our in vitro assembly assay provides an easy and efficient means of screening for assembly inhibitors, and we have identified several inhibitory peptides that could represent a starting point for drug design.
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What OpenQuestion holds
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.