ArticleNature communications2017
Electro-osmotic capture and ionic discrimination of peptide and protein biomarkers with FraC nanopores.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 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
117 citing papers in PubMed.
- Label-Free Profiling of Immunoglobulin Isotypes Using Solid-State Nanopores.Small methods · 2026Article
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- Epx4 Nanopore With Multiple Constrictions for Single-Molecule Identification.Small methods · 2026Article
- Electroosmotic Flow-Driven Nanopore Translocation of Large, Conformationally Dynamic Proteins: Overcoming Steric and Electrostatic Barriers.Journal of the American Chemical Society · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Review
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Selective and Controllable Trapping of Single Proteins in Nanopores Using Reversible Covalent Bonds.ACS nano · 2026Article
- Single-Molecule Discrimination of Multisialylated Ganglioside Oligosaccharides Using an Engineered Nanopore.Research (Washington, D.C.) · 2026Article
- De Novo Design of α-helical Peptide Nanopores for Single-Molecule Detection Using Helix Packing Motifs.ACS nano · 2025Article
- 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
- Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.The Journal of membrane biology · 2025Review
- Single-Molecule Enzyme Activity Analysis for Illuminating Pathological Proteoforms.ACS central science · 2025Review
- Native globular ferritin nanopore sensor.Nature communications · 2025Article
- Single-molecule nanopore sensing of prolineChemical science · 2025Article
- Controlled Sensing of User-Defined Aptamer-Based Targets Using Scanning Ionic Conductance Spectroscopy.ACS nano · 2025Article
- Nanopore sensing of protein and peptide conformation for point-of-care applications.Nature communications · 2025Review
- Redesign of Translocon EXP2 Nanopore for Detecting Peptide Fragments.Small methods · 2025Article
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
57 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.
Funding
Abstract
Biological nanopores are nanoscale sensors employed for high-throughput, low-cost, and long read-length DNA sequencing applications. The analysis and sequencing of proteins, however, is complicated by their folded structure and non-uniform charge. Here we show that an electro-osmotic flow through Fragaceatoxin C (FraC) nanopores can be engineered to allow the entry of polypeptides at a fixed potential regardless of the charge composition of the polypeptide. We further use the nanopore currents to discriminate peptide and protein biomarkers from 25 kDa down to 1.3 kDa including polypeptides differing by one amino acid. On the road to nanopore proteomics, our findings represent a rationale for amino-acid analysis of folded and unfolded polypeptides with nanopores.Biological nanopore-based protein sequencing and recognition is challenging due to the folded structure or non-uniform charge of peptides. Here the authors show that engineered FraC nanopores can overcome these problems and recognize biomarkers in the form of oligopeptides, polypeptides and folded proteins.
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What Socratic 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 Socratic graph.