ArticleNature biotechnology2024
Translocation of linearized full-length proteins through an engineered nanopore under opposing electrophoretic force.
Article in Nature biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed.
- Review
- Article
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- From DNA to full-length proteins through nanopore sequencing.Nature nanotechnology · 2026Article
- An engineered nanopore identifies saccharides, amino acids, peptides and ribonucleotides.Nature biotechnology · 2026Article
- Exopeptidase-assisted nanopore peptide sequence identification.Nature communications · 2026Article
- Single-Molecule Fingerprinting of Unlabeled Full-Length Proteins Using an Aerolysin Nanopore.Journal of the American Chemical Society · 2026Article
- Epx4 Nanopore With Multiple Constrictions for Single-Molecule Identification.Small methods · 2026Article
- High-resolution nanopore peptide sensing, profiling and sequence assembly.Nature nanotechnology · 2026Article
- High-Rate Fingerprinting of Protein Isoforms by Quasi-regulated Enzyme-free Transport Through CytK Nanopores.Research square · 2026Article
- Improving All-Atom Molecular Dynamics Models for Quantitative Prediction of Nanopore Blockade Current.bioRxiv : the preprint server for biology · 2026Article
- Electroosmotic Flow-Driven Nanopore Translocation of Large, Conformationally Dynamic Proteins: Overcoming Steric and Electrostatic Barriers.Journal of the American Chemical Society · 2026Article
- In situ and real-time monitoring of intracellular activities in single live cells using a nanopore probe.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Proteoforms as the true units of physiological function.European journal of applied physiology · 2026Review
- Review
- A stochastic mechanism drives fast substrate translocation in the AAA+ machine ClpB.Nature communications · 2026Article
- Expression and Purification of CytK Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Tuning Rectification and Gating in Biological Nanopores Through Lumen Charge Mutation.Methods in molecular biology (Clifton, N.J.) · 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
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.
Funding
Abstract
Nanopores have recently been used to identify and fingerprint proteins. However, because proteins, unlike DNA, do not have a uniform charge, the electrophoretic force cannot in general be used to translocate or linearize them. Here we show that the introduction of sets of charges in the lumen of the CytK nanopore spaced by ~1 nm creates an electroosmotic flow that induces the unidirectional transport of unstructured natural polypeptides against a strong electrophoretic force. Molecular dynamics simulations indicate that this electroosmotic-dominated force has a strength of ~20 pN at -100 mV, which is similar to the electric force on single-stranded DNA. Unfolded polypeptides produce current signatures as they traverse the nanopore, which may be used to identify proteins. This approach can be used to translocate and stretch proteins for enzymatic and non-enzymatic protein identification and sequencing.
Indexed as
Identifiers
37723268What 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.