ArticleNature biotechnology2023
Unidirectional single-file transport of full-length proteins through a nanopore.
Article in Nature biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 75 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.
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
75 citing papers in PubMed, 122 citations in OpenAlex.
- Review
- From DNA to full-length proteins through nanopore sequencing.Nature nanotechnology · 2026Article
- Article
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- An engineered nanopore identifies saccharides, amino acids, peptides and ribonucleotides.Nature biotechnology · 2026Article
- Nanopore-enabled time-resolved monitoring of catecholamine-related phenylalanine metabolism.Nature nanotechnology · 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
- Engineering a Biological Nanopore for Monitoring Protein Dynamics and Conformational Changes at the Single-Molecule Level.ACS nano · 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
- Heterogeneous Multilayer Nanopores via Chemically Tuned Dielectric Breakdown for Single-Molecule Sensing.Small (Weinheim an der Bergstrasse, Germany) · 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
- Digital Immunoassays for Sensitive Quantification of Blood Biomarkers Using Solid-State Nanopores.ACS nano · 2026Article
- Single-molecule peptide sequencing through reverse translation of peptides into DNA.Nature biotechnology · 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
- Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.Nanoscale · 2026Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The electrical current blockade of a peptide or protein threading through a nanopore can be used as a fingerprint of the molecule in biosensor applications. However, threading of full-length proteins has only been achieved using enzymatic unfolding and translocation. Here we describe an enzyme-free approach for unidirectional, slow transport of full-length proteins through nanopores. We show that the combination of a chemically resistant biological nanopore, α-hemolysin (narrowest part is ~1.4 nm in diameter), and a high concentration guanidinium chloride buffer enables unidirectional, single-file protein transport propelled by an electroosmotic effect. We show that the mean protein translocation velocity depends linearly on the applied voltage and translocation times depend linearly on length, resembling the translocation dynamics of ssDNA. Using a supervised machine-learning classifier, we demonstrate that single-translocation events contain sufficient information to distinguish their threading orientation and identity with accuracies larger than 90%. Capture rates of protein are increased substantially when either a genetically encoded charged peptide tail or a DNA tag is added to a protein.
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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.