ArticlePLoS biology2019
Structures suggest a mechanism for energy coupling by a family of organic anion transporters.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
32 citing papers in PubMed.
- Proton-coupled alternating access in a versatile mycobacterial Spns drug transporter.Research square · 2026Article
- Proton-coupled alternating access in a versatile mycobacterial Spns drug transporter.bioRxiv : the preprint server for biology · 2026Article
- Protonation-dependent substrate release in a bacterial homolog of vesicular glutamate.Biophysical journal · 2026Article
- Memorization bias impacts modeling of alternative conformational states of solute carrier membrane proteins with methods from deep learning.PLoS computational biology · 2025Article
- Ion Translocation Driven by Electric Field Generated in Excited-State Reactions.Accounts of chemical research · 2025Article
- Modeling protein conformational ensembles by guiding AlphaFold2 with Double Electron Electron Resonance (DEER) distance distributions.Nature communications · 2025Article
- Substrate recognition and allosteric regulation of synaptic vesicle glutamate transporter VGLUT2.Nature structural & molecular biology · 2025Article
- Memorization Bias Impacts Modeling of Alternative Conformational States of Symmetric Solute Carrier Membrane Proteins with Methods from Deep Learning.bioRxiv : the preprint server for biology · 2025Article
- Transport mechanism of DgoT, a bacterial homolog of SLC17 organic anion transporters.The EMBO journal · 2024Article
- The human VGLUT3-pT8I mutation elicits uneven striatal DA signaling, food or drug maladaptive consumption in male mice.Nature communications · 2024Article
- Structure and inhibition of the human lysosomal transporter Sialin.Nature communications · 2024Article
- Article
- An efflux pump in genomic island GI-M202a mediates the transfer of polymyxin B resistance in Pandoraea pnomenusa M202.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Review
- Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410.Nature communications · 2023Article
- Structural basis of lipid head group entry to the Kennedy pathway by FLVCR1.bioRxiv : the preprint server for biology · 2023Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
- The molecular mechanism of sialic acid transport mediated by Sialin.Science advances · 2023Article
- The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.Membranes · 2022Article
- Proton-driven alternating access in a spinster lipid transporter.Nature communications · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane.
Indexed as
Identifiers
What OpenQuestion holds
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.