ArticleJournal of virology2005
Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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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
68 citing papers in PubMed, 151 citations in OpenAlex.
- Comparison, Analysis, and Molecular Dynamics Simulations of Structures of a Viral Protein Modeled Using Various Computational Tools.Bioengineering (Basel, Switzerland) · 2023Article
- Production and characterization of monoclonal antibodies for the detection of the hepatitis C core antigen.Frontiers in molecular biosciences · 2023Article
- Domain 2 of Hepatitis C Virus Protein NS5A Activates Glucokinase and Induces Lipogenesis in Hepatocytes.International journal of molecular sciences · 2022Article
- Hepatitis C virus induces oxidation and degradation of apolipoprotein B to enhance lipid accumulation and promote viral production.PLoS pathogens · 2021Article
- Nanosized Particles Assembled by a Recombinant Virus Protein Are Able to Encapsulate Negatively Charged Molecules and Structured RNA.Polymers · 2021Article
- HCV Assembly and Egress via Modifications in Host Lipid Metabolic Systems.Cold Spring Harbor perspectives in medicine · 2021Review
- Review
- Effect of P-body component Mov10 on HCV virus production and infectivity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Very-long-chain fatty acid metabolic capacity of 17-beta-hydroxysteroid dehydrogenase type 12 (HSD17B12) promotes replication of hepatitis C virus and related flaviviruses.Scientific reports · 2020Article
- Hepatitis C Virus Structure: Defined by What It Is Not.Cold Spring Harbor perspectives in medicine · 2020Review
- Virus-induced p38 MAPK activation facilitates viral infection.Theranostics · 2020Article
- Modulation of calcium signaling pathway by hepatitis C virus core protein stimulates NLRP3 inflammasome activation.PLoS pathogens · 2019Article
- Binding of cellular nucleolin with the viral core RNA G-quadruplex structure suppresses HCV replication.Nucleic acids research · 2019Article
- Hepatitis C virus core protein modulates several signaling pathways involved in hepatocellular carcinoma.World journal of gastroenterology · 2019Review
- Methods for Lipid Droplet Biophysical Characterization inFrontiers in microbiology · 2018Review
- Polymorphisms in the hepatitis C virus core and its association with development of hepatocellular carcinoma.Journal of biosciences · 2017Review
- Oxidative stress, a trigger of hepatitis C and B virus-induced liver carcinogenesis.Oncotarget · 2017Review
- A structural perspective of RNA recognition by intrinsically disordered proteins.Cellular and molecular life sciences : CMLS · 2016Review
- Identification of novel RNA secondary structures within the hepatitis C virus genome reveals a cooperative involvement in genome packaging.Scientific reports · 2016Article
- Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A.PLoS pathogens · 2016Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The building block of hepatitis C virus (HCV) nucleocapsid, the core protein, together with viral RNA, is composed of different domains involved in RNA binding and homo-oligomerization. The HCV core protein 1-169 (C(HCV)169) and its N-terminal region from positions 1 to 117 (C(HCV)117) were expressed in Escherichia coli and purified to homogeneity suitable for biochemical and biophysical characterizations. The overall conformation and the oligomeric properties of the resulting proteins C(HCV)169 and C(HCV)117 were investigated by using analytical centrifugation, circular dichroism, intrinsic fluorescence measurements, and limited proteolysis. Altogether, our results show that core protein (C(HCV)169) behaves as a membranous protein and forms heterogeneous soluble micelle-like aggregates of high molecular weight in the absence of detergent. In contrast, it behaves, in the presence of mild detergent, as a soluble, well-folded, noncovalent dimer. Similar to findings observed for core proteins of HCV-related flaviviruses, the HCV core protein is essentially composed of alpha-helices (50%). In contrast, C(HCV)117 is soluble and monodispersed in the absence of detergent but is unfolded. It appears that the folding of the highly basic domain from positions 2 to 117 (2-117 domain) depends on the presence of the 117-169 hydrophobic domain, which contains the structural determinants ensuring the binding of core with cellular membranes. Finally, our findings provide valuable information for further investigations on isolated core protein, as well as for attempts to reconstitute nucleocapsid particles in vitro.
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