Evidence map›Paper›PMID 25599397›Full record

ArticleNature structural & molecular biology2015

Toll-like receptor 8 senses degradation products of single-stranded RNA.

Hiromi Tanji, Umeharu Ohto, Takuma Shibata, Masato Taoka, Yoshio Yamauchi, Toshiaki Isobe, Kensuke Miyake, Toshiyuki Shimizu

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 216 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
216citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

216 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Dissecting the small RNA code of inflammatory bowel disease.Molecular medicine (Cambridge, Mass.) · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Adipose tissue releases nucleosides.American journal of physiology. Cell physiology · 2026
    Article
  19. Review
  20. Wound-Healing Potential of Engineered Lysin GRC-ML07 inAntibiotics (Basel, Switzerland) · 2025
    Article

156 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Hiromi TanjiGraduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan.
Umeharu OhtoGraduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan.
Takuma Shibata1] Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan. [2] Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan.
Masato TaokaDepartment of Chemistry, Graduate School of Science and Technology, Tokyo Metropolitan University, Tokyo, Japan.
Yoshio YamauchiDepartment of Chemistry, Graduate School of Science and Technology, Tokyo Metropolitan University, Tokyo, Japan.
Toshiaki Isobe1] Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan. [2] Department of Chemistry, Graduate School of Science and Technology, Tokyo Metropolitan University, Tokyo, Japan.
Kensuke MiyakeDepartment of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Toshiyuki Shimizu1] Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan. [2] Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Tokyo, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toll-like receptor 8 (TLR8) recognizes viral or bacterial single-stranded RNA (ssRNA) and activates innate immune systems. TLR8 is activated by uridine- and guanosine-rich ssRNA as well as by certain synthetic chemicals; however, the molecular basis for ssRNA recognition has remained unknown. In this study, to elucidate the recognition mechanism of ssRNA, we determined the crystal structures of human TLR8 in complex with ssRNA. TLR8 recognized two degradation products of ssRNA—uridine and a short oligonucleotide—at two distinct sites: uridine bound the site on the dimerization interface where small chemical ligands are recognized, whereas short oligonucleotides bound a newly identified site on the concave surface of the TLR8 horseshoe structure. Site-directed mutagenesis revealed that both binding sites were essential for activation of TLR8 by ssRNA. These results demonstrate that TLR8 is a sensor for both uridine and a short oligonucleotide derived from RNA.

Indexed as

AnimalsBinding SitesCalorimetryCell LineChromatography, LiquidCrystallography, X-RayDrosophilaHumansMass SpectrometryMutagenesis, Site-DirectedProtein Structure, TertiaryRNAToll-Like Receptor 8RNATLR8 protein, humanToll-Like Receptor 8

Identifiers

PMID25599397

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.