ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structural basis for amino acid exchange by a human heteromeric amino acid transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- Selenocystine-based fluorescence assay combined with structural prediction for functional analysis of cystine transporter variants in cystinuria.Journal of Zhejiang University. Science. B · 2026Article
- Potential role of L-citrulline in regulating exercise performance and muscle protein metabolism.NPJ science of food · 2026Review
- Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus.Nature communications · 2026Article
- Arginine Transporters in Human Cancers: Emerging Mechanisms and Clinical Implications.Biomolecules · 2026Review
- Integrative pan-cancer analysis reveals the prognostic and immunological significance of SLC7 family cationic amino acid transporters.Scientific reports · 2026Article
- Structural insights into cationic amino acid transport and viral receptor engagement by CAT1.Nature communications · 2025Article
- Differential uptake of arginine derivatives by the human heteromeric amino acid transporter bNaunyn-Schmiedeberg's archives of pharmacology · 2025Article
- A Review on the Role of Human Solute Carriers Transporters in Cancer.Health science reports · 2025Article
- Mechanisms involved in aminoacidurias: impacts of genetic and environmental factors.Current research in physiology · 2025Review
- The conserved lysine residue in transmembrane helix 5 is pivotal for the cytoplasmic gating of the L-amino acid transporters.PNAS nexus · 2025Article
- SLC7A9 suppression increases chemosensitivity by inducing ferroptosis via the inhibition of cystine transport in gastric cancer.EBioMedicine · 2024Article
- Bacillus CotA laccase improved the intestinal health, amino acid metabolism and hepatic metabolic capacity of Pekin ducks fed naturally contaminated AFBJournal of animal science and biotechnology · 2024Article
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- Structure and mechanisms of transport of human Asc1/CD98hc amino acid transporter.Nature communications · 2024Article
- Osmotic Pressure and Its Biological Implications.International journal of molecular sciences · 2024Review
- Molecular Variability in Levodopa Absorption and Clinical Implications for the Management of Parkinson's Disease.Journal of Parkinson's disease · 2024Review
- Investigation of molecular details of a bacterial cationic amino acid transporter (GkApcT) during arginine transportation using molecular dynamics simulation and umbrella sampling techniques.Journal of molecular modeling · 2023Article
- Interpretation of SLC3A1 and SLC7A9 variants in cystinuria patients: The significance of the PM3 criterion and protein stability.Urolithiasis · 2023Article
- Article
- Effects of arginine replacement with L-citrulline on the arginine/nitric oxide metabolism in chickens: An animal model without urea cycle.Journal of animal science and biotechnology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heteromeric amino acid transporters (HATs) comprise a group of membrane proteins that belong to the solute carrier (SLC) superfamily. They are formed by two different protein components: a light chain subunit from an SLC7 family member and a heavy chain subunit from the SLC3 family. The light chain constitutes the transport subunit whereas the heavy chain mediates trafficking to the plasma membrane and maturation of the functional complex. Mutation, malfunction, and dysregulation of HATs are associated with a wide range of pathologies or represent the direct cause of inherited and acquired disorders. Here we report the cryogenic electron microscopy structure of the neutral and basic amino acid transport complex (b
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