ArticleScience advances2019
RNA binding activates RIG-I by releasing an autorepressed signaling domain.
Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The trial behind it
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- A RIG-I targeting nanozyme induces PANoptosis for cancer immunotherapy.Nature communications · 2026Article
- A20 as a Potential Therapeutic Target for COVID-19.Immunity, inflammation and disease · 2025Review
- Proofreading mechanisms of the innate immune receptor RIG-I: distinguishing self and viral RNA.Biochemical Society transactions · 2024Review
- The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization.Nature communications · 2023Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- Characterization of RNA driven structural changes in full length RIG-I leading to its agonism or antagonism.Nucleic acids research · 2023Article
- The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.Molecular cell · 2022Article
- The intrinsically disordered CARDs-Helicase linker in RIG-I is a molecular gate for RNA proofreading.The EMBO journal · 2022Article
- The nuclear and cytoplasmic activities of RNA polymerase III, and an evolving transcriptome for surveillance.Nucleic acids research · 2021Article
- The molecular mechanism of RIG-I activation and signaling.Immunological reviews · 2021Review
- FIP200 restricts RNA virus infection by facilitating RIG-I activation.Communications biology · 2021Article
- Structural basis for IFN antagonism by human respiratory syncytial virus nonstructural protein 2.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The role of NMolecular cancer · 2020Review
- Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The retinoic acid-inducible gene I (RIG-I) innate immune receptor is an important immunotherapeutic target, but we lack approaches for monitoring the physical basis for its activation in vitro. This gap in our understanding has led to confusion about mechanisms of RIG-I activation and difficulty discovering agonists and antagonists. We therefore created a novel fluorescence resonance energy transfer-based method for measuring RIG-I activation in vitro using dual site-specific fluorescent labeling of the protein. This approach enables us to measure the conformational change that releases the signaling domain during the first step of RIG-I activation, making it possible to understand the role of stimulatory ligands. We have found that RNA alone is sufficient to eject the signaling domain, ejection is reversible, and adenosine triphosphate plays but a minor role in this process. These findings help explain RIG-I dysfunction in autoimmune disease, and they inform the design of therapeutics targeting RIG-I.
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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.