Evidence map›Paper›PMID 30181291›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.

Yuan-Wei Zhang, Sotiria Tavoulari, Steffen Sinning, Antoniya A Aleksandrova, Lucy R Forrest, Gary Rudnick

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Cytosolic KJournal of chemical theory and computation · 2026
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  8. Control of Conformational Transitions by the Conserved GXInternational journal of molecular sciences · 2025
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  12. Identification of the potassium-binding site in serotonin transporter.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  20. Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 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

6 authors at 2 institutions in 2 countries.

Yuan-Wei ZhangDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520-8066.
Sotiria TavoulariDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520-8066.
Steffen SinningDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520-8066.
Antoniya A AleksandrovaComputational Structural Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Lucy R ForrestComputational Structural Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.ORCID 0000-0003-1855-7985
Gary RudnickDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06520-8066; gary.rudnick@yale.edu.ORCID 0000-0002-7622-4110
Yale University · USNational Institutes of Health · US

Funding

Computational Studies of Membrane Transport ProteinsZIANS003139 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI FORREST, LUCY · 2014 to 2025
$13.7M
ION AND BIOGENIC AMINE TRANSPORT MECHANISMSR01DA007259 · NIDA · YALE UNIVERSITY · PI RUDNICK, GARY W · 1992 to 2016
$4.7M
NEUROTRANSMITTER TRANSPORTR01DA008213 · NIDA · YALE UNIVERSITY · PI RUDNICK, GARY W · 1993 to 2014
$3.5M
Conformational change in NSS transportersR01NS102277 · NINDS · YALE UNIVERSITY · PI RUDNICK, GARY W · 2017 to 2020
$2.1M
NIDA NIH HHS R01 DA007259NIDA NIH HHS R01 DA008213NINDS NIH HHS R01 NS102277
6 · The paper itself

Abstract

The coupled transport of ions and substrates allows transporters to accumulate substrates using the energy of transmembrane ion gradients and electrical potentials. During transport, conformational changes that switch accessibility of substrate and ion binding sites from one side of the membrane to the other must be controlled so as to prevent uncoupled movement of ions or substrates. In the neurotransmitter:sodium symporter (NSS) family, Na

Indexed as

Protein DomainsBinding SitesCations, MonovalentCell MembraneCysteineCytoplasmEscherichia coliEscherichia coli ProteinsMolecular Dynamics SimulationMutationPlasma Membrane Neurotransmitter Transport ProteinsProtein BindingSodiumTranscytosisTyrosineCations, MonovalentCysteineEscherichia coli ProteinsPlasma Membrane Neurotransmitter Transport ProteinsSodiumTyrosinecouplingmechanismneurotransmittertransport

Identifiers

PMID30181291
PMCPMC6156673
OpenAlexW2793343697

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.