ReviewThe Journal of physiology2014
How LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transporters.
Review in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 112 citations in OpenAlex.
- An Orchestrated Interaction Network at the Binding Site of Human SERT Enables the Serotonin Occlusion and Import.Biochemistry · 2025Article
- Substrate Binding and Conformational Dynamics of the Monoamine Transporters.Advances in neurobiology · 2025Review
- Monitoring conformational changes in the human neurotransmitter transporter homologue LeuT withJournal of neurochemistry · 2025Article
- Pharmacological Mechanisms of SLC6 Neurotransmitter Transporter Inhibition.Advances in neurobiology · 2025Review
- (-)-Syringaresinol Exerts an Antidepressant-like Activity in Mice by Noncompetitive Inhibition of the Serotonin Transporter.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Alternating access of a bacterial homolog of neurotransmitter: sodium symporters determined from AlphaFold2 ensembles and DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular mechanisms of NaBiophysical journal · 2024Article
- ProteoMutaMetrics: machine learning approaches for solute carrier family 6 mutation pathogenicity prediction.RSC advances · 2024Article
- Conservation of knotted and slipknotted topology in transmembrane transporters.Biophysical journal · 2023Article
- Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.Nature communications · 2023Article
- Overview of the structure and function of the dopamine transporter and its protein interactions.Frontiers in physiology · 2023Review
- Structural Pharmacology of Cation-Chloride Cotransporters.Membranes · 2022Review
- Structural mechanism of SGLT1 inhibitors.Nature communications · 2022Article
- Transmembrane helices 5 and 12 control transport dynamics, substrate affinity, and specificity in the elevator-type UapA transporter.Genetics · 2022Article
- Structure of the human cation-chloride cotransport KCC1 in an outward-open state.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Structural basis for inhibition of the Cation-chloride cotransporter NKCC1 by the diuretic drug bumetanide.Nature communications · 2022Article
- How lipids affect the energetics of co-translational alpha helical membrane protein folding.Biochemical Society transactions · 2022Review
- The Lepidopteran KAAT1 and CAATCH1: Orthologs to Understand Structure-Function Relationships in Mammalian SLC6 Transporters.Neurochemical research · 2022Article
- Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurotransmitter transporters are ion-coupled symporters that drive the uptake of neurotransmitters from neural synapses. In the past decade, the structure of a bacterial amino acid transporter, leucine transporter (LeuT), has given valuable insights into the understanding of architecture and mechanism of mammalian neurotransmitter transporters. Different conformations of LeuT, including a substrate-free state, inward-open state, and competitive and non-competitive inhibitor-bound states, have revealed a mechanistic framework for the transport and transport inhibition of neurotransmitters. The current review integrates our understanding of the mechanistic and pharmacological properties of eukaryotic neurotransmitter transporters obtained through structural snapshots of LeuT.
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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.