Evidence map›Paper›PMID 34360878›Full record

ArticleInternational journal of molecular sciences2021

Novel High Affinity Sigma-1 Receptor Ligands from Minimal Ensemble Docking-Based Virtual Screening.

Szabolcs Dvorácskó, László Lázár, Ferenc Fülöp, Márta Palkó, Zita Zalán, Botond Penke, Lívia Fülöp, Csaba Tömböly, Ferenc Bogár

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

9 authors at 2 institutions in 1 country.

Szabolcs DvorácskóBiological Research Centre, Institute of Biochemistry, Eötvös Loránd Research Network (ELKH), H-6726 Szeged, Hungary.
László LázárInstitute of Pharmaceutical Chemistry, University of Szeged, H-6720 Szeged, Hungary.ORCID 0000-0002-2135-8496
Ferenc FülöpInstitute of Pharmaceutical Chemistry, University of Szeged, H-6720 Szeged, Hungary.ORCID 0000-0003-1066-5287
Márta PalkóInstitute of Pharmaceutical Chemistry, University of Szeged, H-6720 Szeged, Hungary.ORCID 0000-0002-8265-7377
Zita ZalánInstitute of Pharmaceutical Chemistry, University of Szeged, H-6720 Szeged, Hungary.
Botond PenkeDepartment of Medical Chemistry, University of Szeged, H-6720 Szeged, Hungary.
Lívia FülöpDepartment of Medical Chemistry, University of Szeged, H-6720 Szeged, Hungary.ORCID 0000-0002-8010-0129
Csaba TömbölyBiological Research Centre, Institute of Biochemistry, Eötvös Loránd Research Network (ELKH), H-6726 Szeged, Hungary.ORCID 0000-0002-2609-2498
Ferenc BogárDepartment of Medical Chemistry, University of Szeged, H-6720 Szeged, Hungary.
University of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

Nemzeti Kutatási Fejlesztési és Innovációs Hivatal GINOP-2.3.2-15-2016-00034Nemzeti Kutatási Fejlesztési és Innovációs Hivatal GINOP-2.3.2-15-2016-00060
6 · The paper itself

Abstract

Sigma-1 receptor (S1R) is an intracellular, multi-functional, ligand operated protein that also acts as a chaperone. It is considered as a pluripotent drug target in several pathologies. The publication of agonist and antagonist bound receptor structures has paved the way for receptor-based in silico drug design. However, recent studies on this subject payed no attention to the structural differences of agonist and antagonist binding. In this work, we have developed a new ensemble docking-based virtual screening protocol utilizing both agonist and antagonist bound S1R structures. This protocol was used to screen our in-house compound library. The S1R binding affinities of the 40 highest ranked compounds were measured in competitive radioligand binding assays and the sigma-2 receptor (S2R) affinities of the best S1R binders were also determined. This way three novel high affinity S1R ligands were identified and one of them exhibited a notable S1R/S2R selectivity.

Indexed as

Binding SitesHydrophobic and Hydrophilic InteractionsIsoxazolesLigandsMolecular Docking SimulationMolecular StructurePentazocineProtein BindingPyridinesRadioligand AssayReceptors, sigmaSigma-1 Receptor1-propyl-5-(3-p-tolylisoxazol-5-yl)-1,2,3,6-tetrahydropyridineIsoxazolesLigandsPentazocinePyridinesReceptors, sigmaSigma-1 Receptorsigma-2 receptorensemble dockingnovel sigma-1 receptor ligandsradioligand binding assayvirtual screening protocol

Identifiers

PMID34360878
PMCPMC8347176
OpenAlexW3184710070

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.