ArticleProceedings of the National Academy of Sciences of the United States of America2003
Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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
67 citing papers in PubMed, 148 citations in OpenAlex.
- Mechanistic insights into water transport in electrified desalination: Osmosis and electroosmosis decoupled.Science advances · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Single-Molecule Discrimination of Multisialylated Ganglioside Oligosaccharides Using an Engineered Nanopore.Research (Washington, D.C.) · 2026Article
- Comparison among Amber-ff14SB, Amber-ff19SB, and CHARMM36 Force Fields for Ionic and Electroosmotic Flows in Biological Nanopores.Journal of chemical theory and computation · 2025Article
- Understanding single-molecule reactions using nanopore-based techniques.Nature chemistry · 2025Review
- Vectorial Discrimination of Small Molecules with a Macrocycle Adaptor-Protein Nanopore System and Nanocavity-Dependent, pH Gradient-Controlled Analyte Kinetics.Analytical chemistry · 2025Article
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
- Location of Phosphorylation Sites within Long Polypeptide Chains by Binder-Assisted Nanopore Detection.Journal of the American Chemical Society · 2024Article
- Translocation of linearized full-length proteins through an engineered nanopore under opposing electrophoretic force.Nature biotechnology · 2024Article
- Controlling DNA Fragments Translocation across Nanopores with the Synergic Use of Site-Directed Mutagenesis, pH-Dependent Charge Tuning, and Electroosmotic Flow.ACS applied materials & interfaces · 2024Article
- Understanding Electrophoresis and Electroosmosis in Nanopore Sensing with the Help of the Nanopore Electro-Osmotic Trap.ACS nano · 2024Article
- Electro-osmotic Flow Generation via a Sticky Ion Action.ACS nano · 2024Article
- Enzyme-less nanopore detection of post-translational modifications within long polypeptides.Nature nanotechnology · 2023Article
- Multi-pass, single-molecule nanopore reading of long protein strands with single-amino acid sensitivity.bioRxiv : the preprint server for biology · 2023Article
- An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport.Chemical science · 2022Article
- Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021Review
- The Manipulation of the Internal Hydrophobicity of FraC Nanopores Augments Peptide Capture and Recognition.ACS nano · 2021Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
7 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
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flux of solvent water coupled to the transit of ions through protein pores is considerable. The effect of this electroosmotic solvent flow on the binding of a neutral molecule [beta-cyclodextrin (betaCD)] to sites within the staphylococcal alpha-hemolysin pore was investigated. Mutant alpha-hemolysin pores were used to which betaCD can bind from either entrance and through which the direction of water flow can be controlled by choosing the charge selectivity of the pore and the polarity of the applied potential. The Kd values for betaCD for individual mutant pores varied by >100-fold with the applied potential over a range of -120 to +120 mV. In all cases, the signs of the changes in binding free energy and the influence of potential on the association and dissociation rate constants for betaCD were consistent with an electroosmotic effect.
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.