ReviewStructure (London, England : 1993)2013
Neurotransmitter transporters: structure meets function.
Review in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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.
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.
Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- Brain Extracellular Space: From an Overlooked Dimension to Catalyst of a Novel Neuroscience Paradigm.Cyborg and bionic systems (Washington, D.C.) · 2026Review
- Analysis of High-Risk Neuroblastoma Transcriptome Reveals Gene Co-Expression Signatures and Functional Features.Biology · 2023Article
- Recent Investigations on Neurotransmitters' Role in Acute White Matter Injury of Perinatal Glia and Pharmacotherapies-Glia Dynamics in Stem Cell Therapy.Molecular neurobiology · 2022Review
- The substrate import mechanism of the human serotonin transporter.Biophysical journal · 2022Article
- Review
- The antidepressant drug vilazodone is an allosteric inhibitor of the serotonin transporter.Nature communications · 2021Article
- Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters.Nature communications · 2021Article
- Identification of Yak'sAnimals : an open access journal from MDPI · 2020Article
- Allosteric Modulation of Neurotransmitter Transporters as a Therapeutic Strategy.Trends in pharmacological sciences · 2020Review
- A Perspective: Active Role of Lipids in Neurotransmitter Dynamics.Molecular neurobiology · 2020Review
- Structure Modeling of the Norepinephrine Transporter.Biomolecules · 2020Article
- Hydrogen-Deuterium Exchange Mass-Spectrometry of Secondary Active Transporters: From Structural Dynamics to Molecular Mechanisms.Frontiers in pharmacology · 2020Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Polymer-wrapped single-walled carbon nanotubes: a transformation toward better applications in healthcare.Drug delivery and translational research · 2019Review
- Insights into the mechanism and pharmacology of neurotransmitter sodium symporters.Current opinion in structural biology · 2019Review
- Structure and Gating Dynamics of NaFrontiers in molecular biosciences · 2019Review
- Selective Permeability of Carboxysome Shell Pores to Anionic Molecules.The journal of physical chemistry. B · 2018Article
- Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT.Science advances · 2018Article
- Threonine 67 is a key component in the coupling of the NSS amino acid transporter KAAT1.Biochimica et biophysica acta. Biomembranes · 2018Article
- Thermostabilization and purification of the human dopamine transporter (hDAT) in an inhibitor and allosteric ligand bound conformation.PloS one · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
At synapses, sodium-coupled transporters remove released neurotransmitters, thereby recycling them and maintaining a low extracellular concentration of the neurotransmitter. The molecular mechanism underlying sodium-coupled neurotransmitter uptake is not completely understood. Several structures of homologs of human neurotransmitter transporters have been solved with X-ray crystallography. These crystal structures have spurred a plethora of computational and experimental work to elucidate the molecular mechanism underlying sodium-coupled transport. Here, we compare the structures of GltPh, a glutamate transporter homolog, and LeuT, a homolog of neurotransmitter transporters for the biogenic amines and inhibitory molecules GABA and glycine. We relate these structures to data obtained from experiments and computational simulations, to draw conclusions about the mechanism of uptake by sodium-coupled neurotransmitter transporters. Here, we propose how sodium and substrate binding is coupled and how binding of sodium and substrate opens and closes the gates in these transporters, thereby leading to an efficient coupled transport.
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Identifiers
What OpenQuestion holds
Registered trials
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.