Evidence map›Paper›PMID 12668442›Full record

ArticleBiophysical journal2003

Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.

David C Reeves, Muhammed F R Sayed, Pak-Lee Chau, Kerry L Price, Sarah C R Lummis

Open access · bronzeAbstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

34 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Toward a multiscale modeling framework for understanding serotonergic function.Journal of psychopharmacology (Oxford, England) · 2017
    Review
  6. Article
  7. Article
  8. 5-HT(3) receptors.The Journal of biological chemistry · 2012
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. A cation-pi interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  18. Article
  19. Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008
    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

5 authors at 1 institution in 1 country.

David C ReevesDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1AG, United Kingdom.
Muhammed F R Sayed
Pak-Lee Chau
Kerry L Price
Sarah C R Lummis
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

5-HT(3) receptors demonstrate significant structural and functional homology to other members of the Cys-loop ligand-gated ion channel superfamily. The extracellular domains of these receptors share similar sequence homology (approximately 20%) with Limnaea acetylcholine binding protein, for which an x-ray crystal structure is available. We used this structure as a template for computer-based homology modeling of the 5-HT(3) receptor extracellular domain. AutoDock software was used to dock 5-HT into the putative 5-HT(3) receptor ligand-binding site, resulting in seven alternative energetically favorable models. Residues located no more than 5 A from the docked 5-HT were identified for each model; of these, 12 were found to be common to all seven models with five others present in only certain models. Some docking models reflected the cation-pi interaction previously demonstrated for W183, and data from these and other studies were used to define our preferred models.

Indexed as

Models, MolecularAmino Acid SequenceBinding SitesCarrier ProteinsComputer SimulationExtracellular FluidMolecular Sequence DataProtein BindingProtein ConformationProtein Structure, TertiaryProtein SubunitsReceptors, Serotonin, 5-HT3Reproducibility of ResultsSensitivity and SpecificitySequence AlignmentSequence Analysis, ProteinAChBP protein, LymnaeaCarrier ProteinsProtein SubunitsReceptors, Serotonin, 5-HT3Serotonin Receptor Agonists

Identifiers

PMID12668442
PMCPMC1302800
OpenAlexW1984302804

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.