Evidence map›Paper›PMID 27483231›Full record

ReviewMolecules (Basel, Switzerland)2016

Computational Approaches to Toll-Like Receptor 4 Modulation.

Jean-Marc Billod, Alessandra Lacetera, Joan Guzmán-Caldentey, Sonsoles Martín-Santamaría

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Ginsenoside RhInternational journal of molecular sciences · 2024
    Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Gut Molecules in Cardiometabolic Diseases: The Mechanisms behind the Story.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Ginsenoside Ro, an oleanolic saponin ofJournal of ginseng research · 2022
    Article
  19. Article
  20. HSP60-Derived Peptide as an LPS/TLR4 Modulator: AnFrontiers in cardiovascular medicine · 2022
    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 1 institution in 1 country.

Jean-Marc Billod
Alessandra Lacetera
Joan Guzmán-CaldenteyDepartment of Chemical & Physical Biology, Centro de Investigaciones Biológicas, CIB-CSIC, C/Ramiro de Maeztu 9, 28040 Madrid, Spain. juanguzman@cib.csic.es.
Sonsoles Martín-SantamaríaDepartment of Chemical & Physical Biology, Centro de Investigaciones Biológicas, CIB-CSIC, C/Ramiro de Maeztu 9, 28040 Madrid, Spain. smsantamaria@cib.csic.es.
Centro de Investigaciones Biológicas Margarita Salas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toll-like receptor 4 (TLR4), along with its accessory protein myeloid differentiation factor 2 (MD-2), builds a heterodimeric complex that specifically recognizes lipopolysaccharides (LPS), which are present on the cell wall of Gram-negative bacteria, activating the innate immune response. Some TLR4 modulators are undergoing preclinical and clinical evaluation for the treatment of sepsis, inflammatory diseases, cancer and rheumatoid arthritis. Since the relatively recent elucidation of the X-ray crystallographic structure of the extracellular domain of TLR4, research around this fascinating receptor has risen to a new level, and thus, new perspectives have been opened. In particular, diverse computational techniques have been applied to decipher some of the basis at the atomic level regarding the mechanism of functioning and the ligand recognition processes involving the TLR4/MD-2 system at the atomic level. This review summarizes the reported molecular modeling and computational studies that have recently provided insights into the mechanism regulating the activation/inactivation of the TLR4/MD-2 system receptor and the key interactions modulating the molecular recognition process by agonist and antagonist ligands. These studies have contributed to the design and the discovery of novel small molecules with promising activity as TLR4 modulators.

Indexed as

Computational BiologyCrystallography, X-RayDrug DesignGram-Negative BacteriaHumansLipopolysaccharidesLymphocyte Antigen 96Models, MolecularSmall Molecule LibrariesStructural Homology, ProteinToll-Like Receptor 4LipopolysaccharidesLY96 protein, humanLymphocyte Antigen 96Small Molecule LibrariesTLR4 protein, humanToll-Like Receptor 4computational chemistrydockingdrug designhomology modelingMD simulationsmolecular recognitionTLR4/MD-2 modulatorsToll-like receptor 4virtual screening

Identifiers

PMID27483231
PMCPMC6274477
OpenAlexW2494438678

What OpenQuestion holds

Textmetadata
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.