Evidence map›Paper›PMID 25772514›Full record

ArticleChemMedChem2015

Bioisosteric matrices for ligands of serotonin receptors.

Dawid Warszycki, Stefan Mordalski, Jakub Staroń, Andrzej J Bojarski

Abstract read
In one paragraph

Article in ChemMedChem, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–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

1 citing paper in PubMed.

  1. 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.

Dawid WarszyckiInstitute of Pharmacology, Polish Academy of Sciences, 12 Smetna Street, 31-343 Kraków (Poland).
Stefan Mordalski
Jakub Staroń
Andrzej J Bojarski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The concept of bioisosteric replacement matrices is applied to explore the chemical space of serotonin receptor ligands, aiming to determine the most efficient ways of manipulating the affinity for all 5-HT receptor subtypes. Analysis of a collection of over 1 million bioisosteres of compounds with measured activity towards serotonin receptors revealed that an average of 31 % of the ligands for each target are mutual bioisosteres. In addition, the collected dataset allowed the development of bioisosteric matrices-qualitative and quantitative descriptions of the biological effects of each predefined type of bioisosteric substitution, providing favored paths of modifying the compounds. The concept exemplified here for serotonin receptor ligands can likely be more broadly applied to other target classes, thus representing a useful guide for medicinal chemists designing novel ligands.

Indexed as

Drug DesignHumansLigandsPyridinesReceptors, SerotoninSmall Molecule LibrariesSulfonamidesLigandsPyridinesReceptors, SerotoninSmall Molecule LibrariesSulfonamidesbioisosteric matricesbioisosteric substitutionsbioisosterismchemical spaceserotonin receptors

Identifiers

PMID25772514
PMCPMC4471634

What OpenQuestion holds

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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.