ArticleJournal of virology2009
Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus.
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 116 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
116 citing papers in PubMed, 230 citations in OpenAlex.
- Chemical genetics strategy identifies an HCV NS5A inhibitor with a potent clinical effect.Nature · 2010Trial
- A novel dimerization site in non-structural protein 5A of hepatitis C virus regulates viral replication fitness.PLoS pathogens · 2026Article
- Mass balance study of [Antimicrobial agents and chemotherapy · 2026Article
- Phospholipid-driven conformational switching of HCV NS5A links protein folding to replication membrane remodeling.Science advances · 2026Article
- Innovative Amino-Functionalization of Pyrido[2,3-Pharmaceuticals (Basel, Switzerland) · 2025Article
- A key role for hepatitis C virus NS5A serine 225 phosphorylation revealed by super-resolution microscopy.Scientific reports · 2025Article
- Computational design of potent dimeric phenylthiazole NS5A inhibitors for hepatitis C virus.Scientific reports · 2024Article
- Sub-stoichiometric Modulation of Viral Targets-Potent Antiviral Agents That Exploit Target Vulnerability.ACS medicinal chemistry letters · 2023Article
- NS5A domain I antagonises PKR to facilitate the assembly of infectious hepatitis C virus particles.PLoS pathogens · 2023Article
- Design and Synthesis of Novel Bis-Imidazolyl Phenyl Butadiyne Derivatives as HCV NS5A Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Regulatory Role of Phospholipids in Hepatitis C Virus Replication and Protein Function.Pathogens (Basel, Switzerland) · 2022Review
- The Discovery of Conformationally Constrained Bicyclic Peptidomimetics as Potent Hepatitis C NS5A Inhibitors.ACS medicinal chemistry letters · 2021Article
- NS5A-ISGylation via Lysine 26 Has a Critical Role for Efficient Propagation of Hepatitis C Virus Genotype 2a.The Kobe journal of medical sciences · 2021Article
- A Novel Small Molecule Inhibits Hepatitis C Virus Propagation in Cell Culture.Microbiology spectrum · 2021Article
- Quantifying the Evolutionary Constraints and Potential of Hepatitis C Virus NS5A Protein.mSystems · 2021Article
- Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly SensitiveAngewandte Chemie (International ed. in English) · 2021Article
- A novel substitution in NS5A enhances the resistance of hepatitis C virus genotype 3 to daclatasvir.The Journal of general virology · 2021Article
- ISGylation of Hepatitis C Virus NS5A Protein Promotes Viral RNA Replication via Recruitment of Cyclophilin A.Journal of virology · 2020Article
- Factors Influencing the Prevalence of Resistance-Associated Substitutions in NS5A Protein in Treatment-Naive Patients with Chronic Hepatitis C.Biomedicines · 2020Article
- Phenotypic analysis of mutations at residue 146 provides insights into the relationship between NS5A hyperphosphorylation and hepatitis C virus genome replication.The Journal of general virology · 2020Article
56 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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly.
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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.