ArticleNature communications2020
Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Article
- Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters.Nature structural & molecular biology · 2025Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Structural basis of excitatory amino acid transporter 3 substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conformational free energy landscape of a glutamate transporter and microscopic details of its transport mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Structural basis of the excitatory amino acid transporter 3 substrate recognition.bioRxiv : the preprint server for biology · 2024Article
- Antiviral drug recognition and elevator-type transport motions of CNT3.Nature chemical biology · 2024Article
- Structural basis of the obligatory exchange mode of human neutral amino acid transporter ASCT2.Nature communications · 2024Article
- HS-AFM single-molecule structural biology uncovers basis of transporter wanderlust kinetics.Nature structural & molecular biology · 2024Article
- Review
- Custom Design of a Humidifier Chamber forCrystal growth & design · 2024Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
- Symport and antiport mechanisms of human glutamate transporters.Nature communications · 2023Article
- The power and challenge of lipid (a)symmetry across the membrane and cell.Emerging topics in life sciences · 2023Article
- Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6.Nature communications · 2023Article
- Structural insights into inhibitory mechanism of human excitatory amino acid transporter EAAT2.Nature communications · 2022Article
- Structural basis of ligand binding modes of human EAAT2.Nature communications · 2022Article
- Structural basis of ion - substrate coupling in the NaNature communications · 2022Article
- The archaeal glutamate transporter homologue GltPh shows heterogeneous substrate binding.The Journal of general physiology · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type mechanism, in which a mobile transport domain alternates between inward- and outward-oriented states. Using single-particle cryo-EM we have determined five structures of the glutamate transporter homologue Glt
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