Evidence map›Paper›PMID 27598566›Full record

ArticlePloS one2016

Blocking the Interactions between Calcium-Bound S100A12 Protein and the V Domain of RAGE Using Tranilast.

Jian Wei Chiou, Brian Fu, Ruey-Hwang Chou, Chin Yu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Pathogenic role of S100 proteins in psoriasis.Frontiers in immunology · 2023
    Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. S100A12 in Digestive Diseases and Health: A Scoping Review.Gastroenterology research and practice · 2020
    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

4 authors at 3 institutions in 2 countries.

Jian Wei ChiouDepartment of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.
Brian FuNorthwood High School, Irvine, California, 92620, United States of America.
Ruey-Hwang ChouGraduate Institute of Cancer Biology and Center for Molecular Medicine, China Medical University, Taichung, 40402, Taiwan.
Chin YuDepartment of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.
National Tsing Hua University · TWChina Medical University · TWNorthwood University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The receptor for advanced glycation end products (RAGE), a transmembrane receptor in the immunoglobulin superfamily, is involved in several inflammatory processes. RAGE induces cellular signaling pathways upon binding with various ligands, such as advanced glycation end products (AGEs), β-amyloids, and S100 proteins. The solution structure of S100A12 and the V ligand-binding region of RAGE have been reported previously. Using heteronuclear NMR spectroscopy to conduct 1H-15N heteronuclear single quantum coherence (HSQC) titration experiments, we identified and mapped the binding interface between S100A12 and the V domain of RAGE. The NMR chemical shift data were used as the constraints for the High Ambiguity Driven biomolecular DOCKing (HADDOCK) calculation to generate a structural model of the S100A12-V domain complex. In addition, tranilast (an anti-allergic drug) showed strong interaction with S100A12 in the 1H-15N HSQC titration, fluorescence experiments, and WST-1 assay. The results also indicated that tranilast was located at the binding site between S100A12 and the V domain, blocking interaction between these two proteins. Our results provide the mechanistic details for a structural model and reveal a potential precursor for an inhibitor for pro-inflammatory diseases, which could be useful for the development of new drugs.

Indexed as

Amino Acid MotifsAnti-Allergic AgentsBinding SitesCloning, MolecularEscherichia coliGene ExpressionHumansKineticsMolecular Docking SimulationNuclear Magnetic Resonance, Biomolecularortho-AminobenzoatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsReceptor for Advanced Glycation End ProductsAGER protein, humanAnti-Allergic Agentsortho-AminobenzoatesReceptor for Advanced Glycation End ProductsRecombinant ProteinsS100A12 ProteinS100A12 protein, humantranilast

Identifiers

PMID27598566
PMCPMC5012620
OpenAlexW2511724056

What OpenQuestion holds

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LicenceCC BY
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.