ReviewAAPS pharmSci1999
The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors.
Review in AAPS pharmSci, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 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
99 citing papers in PubMed, 250 citations in OpenAlex.
- Benchmarking AI Protein Structure Predictors Reveals a Persistent Bias in Multi-State Proteins.bioRxiv : the preprint server for biology · 2026Article
- A Thr/Ser-centered phosphate-binding triad of phosphate-binding protein SphX from Synechocystis.Communications biology · 2026Article
- Microscopic Insights into a Ligand Escape Pathway and Energetics in Leucine-Isoleucine-Valine Binding Protein.ACS omega · 2026Article
- A Portable Fluorometer for the Detection of Glyphosate.Biosensors · 2026Article
- Structural basis of FatB-mediated iron uptake via tyrosine/histidine direct coordination accompanying long-distance domain reorganization.Nature communications · 2026Article
- Genetically encoded sensors illuminateIBRO neuroscience reports · 2025Article
- Molecular determinants of Neu5Ac binding to a tripartite ATP independent periplasmic (TRAP) transporter.eLife · 2025Article
- AMPA receptors in the evolving synapse: structure, function, and disease implications.Frontiers in synaptic neuroscience · 2025Review
- On the function of TRAP substrate-binding proteins: the isethionate-specific binding protein IseP.The Biochemical journal · 2024Article
- On the function of TRAP substrate-binding proteins: Conformational variation of the sialic acid binding protein SiaP.The Journal of biological chemistry · 2024Article
- Glutamate, Gangliosides, and the Synapse: Electrostatics at Work in the Brain.International journal of molecular sciences · 2024Review
- Computational design of Periplasmic binding protein biosensors guided by molecular dynamics.PLoS computational biology · 2024Article
- Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023Article
- The phosphodiesterase RmcA contributes to the adaptation of Pseudomonas putida to l-arginine.FEMS microbiology letters · 2023Article
- Structures of permuted halves of a modern ribose-binding protein.Acta crystallographica. Section D, Structural biology · 2023Article
- Sialic Acid 4-N-Piperazine and Piperidine Derivatives Bind with High Affinity to the P. mirabilis Sialic Acid Sodium Solute Symporter.ChemMedChem · 2022Article
- The measurement of binding affinities by NMR chemical shift perturbation.Journal of biomolecular NMR · 2022Article
- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Sensory Perception in Bacterial Cyclic Diguanylate Signal Transduction.Journal of bacteriology · 2022Review
- Evolution of glutamatergic signaling and synapses.Neuropharmacology · 2021Review
39 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
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Located between the inner and outer membranes of Gram-negative bacteria, periplasmic binding proteins (PBPs) scavenge or sense diverse nutrients in the environment by coupling to transporters or chemotaxis receptors in the inner membrane. Their three-dimensional structures have been deduced in atomic detail with the use of X-ray crystallography, both in the free and liganded state. PBPs consist of two large lobes that close around the bound ligand, resembling a Venus flytrap. This architecture is reiterated in transcriptional regulators, such as the lac repressors. In the process of evolution, genes encoding the PBPs have fused with genes for integral membrane proteins. Thus, diverse mammalian receptors contain extracellular ligand binding domains that are homologous to the PBPs; these include glutamate/glycine-gated ion channels such as the NMDA receptor, G protein-coupled receptors, including metabotropic glutamate, GABA-B, calcium sensing, and pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. Many of these receptors are promising drug targets. On the basis of homology to PBPs and a recently resolved crystal structure of the extracellular binding domain of a glutamate receptor ion channel, it is possible to construct three-dimensional models of their ligand binding domains. Together with the extensive information available on the mechanism of ligand binding to PBPs, such models can serve as a guide in drug discovery.
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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.