ArticleImmunity2012
Structure and functional characterization of the RNA-binding element of the NLRX1 innate immune modulator.
Article in Immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 95 citations in OpenAlex.
- Phenotypic CRISPR screens identify NLRX1 as an essential activator of the human mitochondrial permeability transition.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Neuroimmune interactions: The bridge between inflammatory bowel disease and the gut microbiota.Clinical and translational medicine · 2025Review
- Innate Immunity Never "NODs" Off: NLRs Regulate the Host Anti-Viral Immune Response.Immunological reviews · 2025Review
- Pattern Recognition by NOD-Like Receptors.Advances in experimental medicine and biology · 2025Review
- Insights into the structure of NLR family member X1: Paving the way for innovative drug discovery.Computational and structural biotechnology journal · 2024Article
- Article
- A zebrafish NLRX1 isoform downregulates fish IFN responses by targeting the adaptor STING.Journal of virology · 2024Article
- The NLR gene family: from discovery to present day.Nature reviews. Immunology · 2023Review
- Teleost NOD-like receptors and their downstream signaling pathways: A brief review.Fish and shellfish immunology reports · 2022Review
- Immunometabolic rewiring of tubular epithelial cells in kidney disease.Nature reviews. Nephrology · 2022Review
- Cytoplasmic RNA sensors and their interplay with RNA-binding partners in innate antiviral response: theme and variations.RNA (New York, N.Y.) · 2022Review
- Impact of intracellular innate immune receptors on immunometabolism.Cellular & molecular immunology · 2022Review
- Sex-Biased Control of Inflammation and Metabolism by a Mitochondrial Nod-Like Receptor.Frontiers in immunology · 2022Article
- NLR in eXile: Emerging roles of NLRX1 in immunity and human disease.Immunology · 2021Review
- Focusing on the Cell Type Specific Regulatory Actions of NLRX1.International journal of molecular sciences · 2021Review
- Innate Immune Responses and Pulmonary Diseases.Advances in experimental medicine and biology · 2021Article
- NLRX1 is a key regulator of immune signaling during invasive pulmonary aspergillosis.PLoS pathogens · 2020Article
- Review
- Avian Pattern Recognition Receptor Sensing and Signaling.Veterinary sciences · 2020Review
Corrections and comments
- Commented on by
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial NLRX1 is a member of the family of nucleotide-binding domain and leucine-rich-repeat-containing proteins (NLRs) that mediate host innate immunity as intracellular surveillance sensors against common molecular patterns of invading pathogens. NLRX1 functions in antiviral immunity, but the molecular mechanism of its ligand-induced activation is largely unknown. The crystal structure of the C-terminal fragment (residues 629-975) of human NLRX1 (cNLRX1) at 2.65 Å resolution reveals that cNLRX1 consists of an N-terminal helical (LRRNT) domain, central leucine-rich repeat modules (LRRM), and a C-terminal three-helix bundle (LRRCT). cNLRX1 assembles into a compact hexameric architecture that is stabilized by intersubunit and interdomain interactions of LRRNT and LRRCT in the trimer and dimer components of the hexamer, respectively. Furthermore, we find that cNLRX1 interacts directly with RNA and supports a role for NLRX1 in recognition of intracellular viral RNA in antiviral immunity.
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.