ReviewFrontiers in cellular and infection microbiology2023
The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant.
Review in Frontiers in cellular and infection microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.Biochemical Society transactions · 2026Review
- Mechanisms and strategies of host xenophagy manipulation by intracellular bacteria.Cellular and molecular life sciences : CMLS · 2026Review
- RNF213 isoform 2 restricts Zika virus through antiviral signaling and viral protein degradation.iScience · 2026Article
- Coral color morphs exhibit distinct microbial and proteomic profiles linked to stress and immune mechanisms in a changing ocean.Microbiome · 2026Article
- The host ubiquitination system dynamically regulates the inflammatory response of macrophages to bacteria.Frontiers in immunology · 2026Review
- Multisystemic Impact of RNF213 Arg4810Lys: A Comprehensive Review of Moyamoya Disease and Associated Vasculopathies.International journal of molecular sciences · 2025Review
- Review
- RNF213-Dependent EGFR and HER2 Activation Regulates Specific Downstream Signaling Pathways in Human Cancer Cells.Genes to cells : devoted to molecular & cellular mechanisms · 2025Article
- RNF213 Acts as a Molecular Switch for Cav-1 Ubiquitination and Phosphorylation in Human Cells.Cells · 2025Article
- Inc/GFP chimera protein-based interactomics reveals host cellular interactions of Cps0558, a novel Chlamydia psittaci inclusion protein.Pathogens and disease · 2025Article
- ISGylation and E3 ubiquitin ligases: an Atlantic salmon genetic perspective.Frontiers in immunology · 2025Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space. Missense mutations in this gene have been found to be more prevalent in patients with moyamoya disease compared with that in healthy individuals. Understanding the molecular function of RNF213 could provide insights into moyamoya disease. RNF213 contains a C3HC4-type RING finger domain with an E3 ubiquitin ligase domain and six AAA+ adenosine triphosphatase (ATPase) domains. It is the only known protein with both AAA+ ATPase and ubiquitin ligase activities. Recent studies have highlighted the role of RNF213 in fighting against microbial infections, including viruses, parasites, bacteria, and chlamydiae. This review aims to summarize the recent research progress on the mechanisms of RNF213 in pathogenic infections, which will aid researchers in understanding the antimicrobial role of RNF213.
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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.