ReviewFrontiers in immunology2018
RING-Domain E3 Ligase-Mediated Host-Virus Interactions: Orchestrating Immune Responses by the Host and Antagonizing Immune Defense by Viruses.
Review in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- Unveiling novel susceptibility genes for sarcoidosis by a cross-tissue transcriptome-wide association study.Sarcoidosis, vasculitis, and diffuse lung diseases : official journal of WASOG · 2026Article
- SRBSDV-derived small interfering RNAs modulate insect vector reproduction and viral replication in Sogatella furcifera.Communications biology · 2026Article
- STING single amino acid polymorphisms modulate iridovirus immune evasion and pathogenicity spectrum.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Persistent mirusvirus infection in the marine protist Aurantiochytrium.Nature communications · 2025Article
- Ubiquitin E3 ligase MARCH10 targets influenza hemagglutinin for ubiquitination.Cellular signalling · 2025Article
- E3 ubiquitin ligase RNF128 attenuates colitis and colorectal tumorigenesis by triggering the degradation of IL-6 receptors.Journal of advanced research · 2025Article
- Arboviruses antagonize insect Toll antiviral immune signaling to facilitate the coexistence of viruses with their vectors.PLoS pathogens · 2024Article
- Polyubiquitylated rice stripe virus NS3 translocates to the nucleus to promote cytosolic virus replication via miRNA-induced fibrillin 2 upregulation.PLoS pathogens · 2024Article
- Multiple E3 ligases control tankyrase stability and function.Nature communications · 2023Article
- Plasma Proteomics Unveil Novel Immune Signatures and Biomarkers upon SARS-CoV-2 Infection.International journal of molecular sciences · 2023Article
- Emerging Roles of RNF168 in Tumor Progression.Molecules (Basel, Switzerland) · 2023Review
- TRAF6 autophagic degradation byAutophagy · 2022Article
- The RING finger protein family in health and disease.Signal transduction and targeted therapy · 2022Review
- Exploration of nanozymes in viral diagnosis and therapy.Exploration (Beijing, China) · 2022Review
- MRKNs: Gene, Functions, and Role in Disease and Infection.Frontiers in oncology · 2022Review
- An integrative pan-cancer analysis revealing the difference in small ring finger family of SCF E3 ubiquitin ligases.Frontiers in immunology · 2022Article
- Nuclear Import of HIV-1.Viruses · 2021Review
- Article
- Polinton-like viruses are abundant in aquatic ecosystems.Microbiome · 2021Article
- Proteomic Signature of Host Response to SARS-CoV-2 Infection in the Nasopharynx.Molecular & cellular proteomics : MCP · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RING-domain E3 ligases (RING E3s), a group of E3 ligases containing one or two RING finger domains, are involved in various cellular processes such as cell proliferation, immune regulation, apoptosis, among others. In the host, a substantial number of the RING E3s have been implicated to inhibit viral replication through regulating immune responses, including activation and inhibition of retinoic acid-inducible gene I-like receptors, toll-like receptors, and DNA receptor signaling pathways, modulation of cell-surface expression of major histocompatibility complex, and co-stimulatory molecules. During the course of evolution and adaptation, viruses encode RING E3s to antagonize host immune defense, such as the infected cell protein 0 of herpes simplex virus type 1, the non-structural protein 1 of rotavirus, and the K3 and K5 of Kaposi's sarcoma-associated herpesvirus. In addition, recent studies suggest that viruses can hijack the host RING E3s to facilitate viral replication. Based on emerging and interesting discoveries, the RING E3s present novel links among the host and viruses. Herein, we focus on the latest research progresses in the RING E3s-mediated host-virus interactions and discuss the outlooks of the RING E3s for future research.
Indexed as
Identifiers
What OpenQuestion holds
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.