ArticleProceedings of the National Academy of Sciences of the United States of America2019
Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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.
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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.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.Nature communications · 2025Article
- Structure and function of the SIT1 proline transporter in complex with the COVID-19 receptor ACE2.Nature communications · 2024Article
- Transcriptomic insights into the dominance of two phototrophs throughout the water column of a tropical hypersaline-alkaline crater lake (Dziani Dzaha, Mayotte).Frontiers in microbiology · 2024Article
- Modifications to a Biphenolic Antibacterial Compound: Activity against ESKAPE Pathogens.ChemMedChem · 2023Article
- Effect of NaCl stress on exoproteome profiles ofFrontiers in microbiology · 2023Article
- Structural basis for substrate specificity of heteromeric transporters of neutral amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.Communications biology · 2021Article
- Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.Scientific reports · 2020Article
- Structural basis of proton-coupled potassium transport in the KUP family.Nature communications · 2020Article
- Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The amino acid, polyamine, and organocation (APC) superfamily is the second largest superfamily of membrane proteins forming secondary transporters that move a range of organic molecules across the cell membrane. Each transporter in the APC superfamily is specific for a unique subset of substrates, even if they possess a similar structural fold. The mechanism of substrate selectivity remains, by and large, elusive. Here, we report two crystal structures of an APC member from
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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.