ArticleEuropean biophysics journal : EBJ2010
NMR studies of p7 protein from hepatitis C virus.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 61 citations in OpenAlex.
- Review
- Viroporins and inflammasomes: A key to understand virus-induced inflammation.The international journal of biochemistry & cell biology · 2020Review
- Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features.Scientific reports · 2019Article
- Symmetric dimeric adamantanes for exploring the structure of two viroporins: influenza virus M2 and hepatitis C virus p7.Drug design, development and therapy · 2018Article
- Coupling neutron reflectivity with cell-free protein synthesis to probe membrane protein structure in supported bilayers.Scientific reports · 2017Article
- Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico.Biochimica et biophysica acta · 2016Review
- Patch-Clamp Study of Hepatitis C p7 Channels Reveals Genotype-Specific Sensitivity to Inhibitors.Biophysical journal · 2016Article
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- Relating structure and function of viral membrane-spanning miniproteins.Current opinion in virology · 2015Review
- Genotype-specific differences in structural features of hepatitis C virus (HCV) p7 membrane protein.Biochimica et biophysica acta · 2015Article
- Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release.Hepatology (Baltimore, Md.) · 2014Article
- Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release.PloS one · 2014Article
- Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptides.The journal of physical chemistry. B · 2013Article
- Assembling an ion channel: ORF 3a from SARS-CoV.Biopolymers · 2013Article
- Three-dimensional structure and interaction studies of hepatitis C virus p7 in 1,2-dihexanoyl-sn-glycero-3-phosphocholine by solution nuclear magnetic resonance.Biochemistry · 2013Article
- The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivatives.Chemical reviews · 2013Review
- Computational modeling of the p7 monomer from HCV and its interaction with small molecule drugs.SpringerPlus · 2013Article
- Viruses as modulators of mitochondrial functions.Advances in virology · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Proline kink angle distributions for GWALP23 in lipid bilayers of different thicknesses.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The p7 protein of hepatitis C virus (HCV) plays an important role in the viral lifecycle. Like other members of the viroporin family of small membrane proteins, the amino acid sequence of p7 is largely conserved over the entire range of genotypes, and it forms ion channels that can be blocked by a number of established channel-blocking compounds. Its characteristics as a membrane protein make it difficult to study by most structural techniques, since it requires the presence of lipids to fold and function properly. Purified p7 can be incorporated into phospholipid bilayers and micelles. Initial solid-state nuclear magnetic resonance (NMR) studies of p7 in 14-O-PC/6-O-PC bicelles indicate that the protein contains helical segments that are tilted approximately 10 degrees and 25 degrees relative to the bilayer normal. A truncated construct corresponding to the second transmembrane domain of p7 is shown to have properties similar to those of the full-length protein, and was used to determine that the helix segment tilted at 10 degrees is in the C-terminal portion of the protein. The addition of the channel blocker amantadine to the full-length protein resulted in selective chemical shift changes, demonstrating that NMR has a potential role in the development of drugs targeted to p7.
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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.