Evidence map›Paper›PMID 25092290›Full record

ArticleThe Journal of biological chemistry2014

LL-37 peptide enhancement of signal transduction by Toll-like receptor 3 is regulated by pH: identification of a peptide antagonist of LL-37.

Divyendu Singh, Robert Vaughan, C Cheng Kao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 9% of its field
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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Human antimicrobial/host defense peptide LL-37 may prevent the spread of a local infection through multiple mechanisms: an update.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Review
  4. Vitamin D effects onFrontiers in cellular and infection microbiology · 2024
    Article
  5. Article
  6. Synthetic mucus biomaterials for antimicrobial peptide delivery.Journal of biomedical materials research. Part A · 2023
    Article
  7. Review
  8. Synthetic Mucus Biomaterials for Antimicrobial Peptide Delivery.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Vitamin D, infections and immunity.Reviews in endocrine & metabolic disorders · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Recombinant CRAMP-producingFood & nutrition research · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Divyendu SinghFrom the Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405.
Robert VaughanFrom the Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405.
C Cheng KaoFrom the Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405 ckao@indiana.edu.
Indiana University Bloomington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LL-37 is a peptide secreted by human epithelial cells that can lyse bacteria, suppress signaling by Toll-like receptor 4 (TLR4), and enhance signaling to double-stranded RNA (dsRNA) by TLR3. How LL-37 interacts with dsRNA to affect signal transduction by TLR3 is not completely understood. We determined that LL-37 binds dsRNA and traffics to endosomes and releases the dsRNA in a pH-dependent manner. Using dynamic light scattering spectroscopy and cell-based FRET experiments, LL-37 was found to form higher order complexes independent of dsRNA binding. Upon acidification LL-37 will dissociate from a larger complex. In cells, LL-37 has a half-live of ∼ 1 h. LL-37 half-life was increased by inhibiting endosome acidification or inhibiting cathepsins, which include proteases whose activity are activated by endosome acidification. Residues in LL-37 that contact poly(I:C) and facilitate oligomerization in vitro were mapped. Peptide LL-29, which contains the oligomerization region of LL-37, inhibited LL-37 enhancement of TLR3 signal transduction. LL-29 prevented LL-37 · poly(I:C) co-localization to endosomes containing TLR3. These results shed light on the requirements for LL-37 enhancement of TLR3 signaling.

Indexed as

Signal TransductionAmino Acid SequenceAntimicrobial Cationic PeptidesBinding SitesCathelicidinsEndosomesHumansHydrogen-Ion ConcentrationMolecular Sequence DataPeptidesRNA, Double-StrandedToll-Like Receptor 3Up-RegulationAntimicrobial Cationic PeptidesCathelicidinsPeptidesRNA, Double-StrandedTLR3 protein, humanToll-Like Receptor 3EndosomeInnate ImmunitypHpH RegulationRNA-binding ProteinToll-like Receptor (TLR)

Identifiers

PMID25092290
PMCPMC4183800
OpenAlexW2081546869

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.