Evidence map›Paper›PMID 41253806›Full record

ArticleNature communications2025

Structural basis of vilazodone dual binding mode to the serotonin transporter.

Iris E Kalenderoglou, Andreas Nygaard, Caleb D Vogt, Anton Turaev, Tillmann Pape, Nathan B P Adams, Amy Hauck Newman, Claus J Loland

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. 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. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Iris E KalenderoglouDepartment of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0001-8491-2776
Andreas NygaardDepartment of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Caleb D VogtMedicinal Chemistry Section, Molecular Targets and Medications Discovery Branch, National Institute on Drug Abuse - Intramural Research Program, National Institutes of Health, 333 Cassell Drive, Baltimore, MD, US.
Anton TuraevNanoTemper Technologies, Floessegasse 4, Munich, Germany.
Tillmann PapeStructural Molecular Biology Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-0612-3568
Nathan B P AdamsNanoTemper Technologies, Floessegasse 4, Munich, Germany.ORCID http://orcid.org/0000-0003-3080-3448
Amy Hauck NewmanMedicinal Chemistry Section, Molecular Targets and Medications Discovery Branch, National Institute on Drug Abuse - Intramural Research Program, National Institutes of Health, 333 Cassell Drive, Baltimore, MD, US.ORCID http://orcid.org/0000-0002-4812-9474
Claus J LolandDepartment of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. cllo@sund.ku.dk.ORCID http://orcid.org/0000-0002-1773-1446

Funding

SYNTHETIC STRATEGIES TOWARD THE ELUCIDATION OF CENTRAL MECHANISMS IN THE BEHAVIORZ01DA000389 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI NEWMAN, AMY HAUCK · 1996 to 2008
$1.3M
NEUROCHEMISTRY OF AMPHETAMINE INDUCED AROUSALK02DA000389 · NIDA · UNIVERSITY OF WISCONSIN-MADISON · PI BERRIDGE, CRAIG W · 1999 to 2008
$1.1M
Carlsbergfondet (Carlsberg Foundation) CF23-1034EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 Marie Skłodowska-Curie Actions (H2020 Excellent Science - Marie Skłodowska-Curie Actions) 860954Intramural NIH HHS Z01 DA000389NIDA NIH HHS K02 DA000389Novo Nordisk Fonden (Novo Nordisk Foundation) NNF17SA0024386Novo Nordisk Fonden (Novo Nordisk Foundation) NNF220C0079091Novo Nordisk Fonden (Novo Nordisk Foundation) NNF22OC0075808Sundhed og Sygdom, Det Frie Forskningsråd (Medical Sciences, Danish Council for Independent Research) 1030-00036BU.S. Department of Health & Human Services | NIH | National Institute on Drug Abuse (NIDA) Z1A DA000389
6 · The paper itself

Abstract

The serotonin transporter (SERT) plays a pivotal role in regulating serotonin (5-HT) signaling and is a key target in the treatment of psychiatric disorders. SERT has a binding site (S1) for 5-HT that also serves as a high-affinity binding site for antidepressants. The antidepressant vilazodone has been shown to inhibit SERT by binding to an allosteric site. Here, we present the cryo-EM structure of SERT with vilazodone bound to the S1 site and extending towards the allosteric site. We systematically dissect the vilazodone molecule into fragments and find that the terminal indole ring is the key determinant of its high affinity to SERT. Further, unlike typical Na

Indexed as

Serotonin Plasma Membrane Transport ProteinsVilazodone HydrochlorideAllosteric SiteAntidepressive AgentsBinding SitesCryoelectron MicroscopyHumansModels, MolecularProtein BindingSelective Serotonin Reuptake InhibitorsSerotoninAntidepressive AgentsSelective Serotonin Reuptake InhibitorsSerotoninSerotonin Plasma Membrane Transport ProteinsSLC6A4 protein, humanVilazodone Hydrochloride

Identifiers

PMID41253806
PMCPMC12627810

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.