ArticleScience (New York, N.Y.)2009
Structure and mechanism of a Na+-independent amino acid transporter.
Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers, 1 of them a synthesis that pooled it.
What it found
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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
198 citing papers in PubMed, 1 synthesis or guideline pooled it, 317 citations in OpenAlex.
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- Structure and conformational dynamics of the Pseudomonas CbrA transceptor.Protein science : a publication of the Protein Society · 2026Article
- Structural basis for pH-responsive amino acid transport via SLC7A4.Nature communications · 2026Article
- Structure and conformational dynamics of thebioRxiv : the preprint server for biology · 2026Article
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus.Nature communications · 2026Article
- GerAB residues predicted to interact with water based on MD simulations mediate germinosome stability inFrontiers in microbiology · 2026Article
- Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.Nature communications · 2025Article
- Article
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- In silico characterization, structural modeling, and molecular docking of GabP in citrus and its potential role in GABA uptake.Scientific reports · 2025Article
- Examination of conformational dynamics of AdiC transporter with fluorescence-polarization microscopy.The Journal of general physiology · 2025Article
- Generation of Conformation-Specific Monoclonal Antibodies for Integral Membrane Proteins.Current protocols · 2025Article
- Cryo-EM structures reveal the HLife science alliance · 2025Article
- Structural basis of urea transport by Arabidopsis thaliana DUR3.Nature communications · 2025Article
- GerAB residues predicted to interfere with water passage based on steered molecular dynamics are key to germinosome functionality.Frontiers in microbiology · 2025Article
- Navigating the multifaceted intricacies of the NaPhysiological reviews · 2024Review
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- Review
- Magnolol Supplementation Alters Serum Parameters, Immune Homeostasis, Amino Acid Profiles, and Gene Expression of Amino Acid Transporters in Growing Pigs.International journal of molecular sciences · 2023Article
138 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.
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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.