ArticleStructure (London, England : 1993)2014
(19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
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- A naturally occurring NS1 variant with effector domain deletion gains growth advantages in influenza virus infection.Emerging microbes & infections · 2025Article
- Nonstructural Protein 1 of Influenza A (NS1A) Demonstrates Strain-Specific dsRNA Binding Capabilities.ACS infectious diseases · 2025Article
- High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis forAngewandte Chemie (International ed. in English) · 2025Article
- Review
- Micromolar fluoride contamination arising from glass NMR tubes and a simple solution for biomolecular applications.Journal of biomolecular NMR · 2024Article
- The NS1 protein of influenza B virus binds 5'-triphosphorylated dsRNA to suppress RIG-I activation and the host antiviral response.bioRxiv : the preprint server for biology · 2024Article
- Representing structures of the multiple conformational states of proteins.Current opinion in structural biology · 2023Review
- Protein-Engineered Fibers For Drug Encapsulation Traceable viaACS applied nano materials · 2023Article
- Structural Investigations of Interactions between the Influenza a Virus NS1 and Host Cellular Proteins.Viruses · 2023Review
- Assessing the applicability ofJournal of biomolecular NMR · 2023Article
- Interaction of the Influenza A Virus NS1 Protein with the 5'-m7G-mRNA·eIF4E·eIF4G1 Complex.Biochemistry · 2022Article
- Article
- Isotope Labels Combined with Solution NMR Spectroscopy Make Visible the Invisible Conformations of Small-to-Large RNAs.Chemical reviews · 2022Review
- Review
- Structure and Activities of the NS1 Influenza Protein and Progress in the Development of Small-Molecule Drugs.International journal of molecular sciences · 2021Review
- The intracellular environment affects protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- A suite ofJournal of biomolecular NMR · 2020Article
- Homodimerization of a glycoside hydrolase family GH1 β-glucosidase suggests distinct activity of enzyme different states.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Nonstructural protein 1 of influenza A virus (NS1A) is a conserved virulence factor comprised of an N-terminal double-stranded RNA (dsRNA)-binding domain and a multifunctional C-terminal effector domain (ED), each of which can independently form symmetric homodimers. Here we apply (19)F NMR to NS1A from influenza A/Udorn/307/1972 virus (H3N2) labeled with 5-fluorotryptophan, and we demonstrate that the (19)F signal of Trp187 is a sensitive, direct monitor of the ED helix:helix dimer interface. (19)F relaxation dispersion data reveal the presence of conformational dynamics within this functionally important protein:protein interface, whose rate is more than three orders of magnitude faster than the kinetics of ED dimerization. (19)F NMR also affords direct spectroscopic evidence that Trp187, which mediates intermolecular ED:ED interactions required for cooperative dsRNA binding, is solvent exposed in full-length NS1A at concentrations below aggregation. These results have important implications for the diverse roles of this NS1A epitope during influenza virus infection.
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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.