ArticleNature nanotechnology2017
Real-time shape approximation and fingerprinting of single proteins using a nanopore.
Article in Nature nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 173 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.
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Who cites it
173 citing papers in PubMed.
- Review
- Stress-induced ripping enables fabrication of nanopores with dimensions smaller than the resolution limit of the employed lithography.Science advances · 2026Article
- Engineering a Biological Nanopore for Monitoring Protein Dynamics and Conformational Changes at the Single-Molecule Level.ACS nano · 2026Article
- Geometric Confinement in Solid-State Nanopores Enables Single-Molecule Discrimination of Ferritin Subunits and Translocation Bias.Nano letters · 2026Article
- Digital Immunoassays for Sensitive Quantification of Blood Biomarkers Using Solid-State Nanopores.ACS nano · 2026Article
- Article
- Label-Free Optical Differentiation of Single Diffusing Amino Acids at Picomolar Concentrations.Research square · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Ionic species programmable synaptic plasticity in multimodal nanofluidic devices.National science review · 2026Article
- Uncovering Hidden Protein Conformations with High Bandwidth Nanopore Measurements.Nano letters · 2026Article
- Review
- Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores.Nanoscale · 2026Article
- Continuous, Low Latency Estimation of the Size and Shape of Single Proteins from Real-Time Nanopore Data.Analytical chemistry · 2026Article
- Selective and Controllable Trapping of Single Proteins in Nanopores Using Reversible Covalent Bonds.ACS nano · 2026Article
- Threading of Single Protein Molecules Through a Solid-State Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Metrology of Nanoscale Objects Using Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Voltage-matrix nanopore profiling for the discrimination of protein mixtures.Chemical science · 2025Article
- Full-length protein classification via cysteine fingerprinting in solid-state nanopores.Nature nanotechnology · 2025Article
- Universal Nanopore Sensor for Amplification-Free and Label-Free Detection of Molecular Biomarkers.ACS sensors · 2025Article
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
113 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
13 authors.
Funding
Abstract
Established methods for characterizing proteins typically require physical or chemical modification steps or cannot be used to examine individual molecules in solution. Ionic current measurements through electrolyte-filled nanopores can characterize single native proteins in an aqueous environment, but currently offer only limited capabilities. Here we show that the zeptolitre sensing volume of bilayer-coated solid-state nanopores can be used to determine the approximate shape, volume, charge, rotational diffusion coefficient and dipole moment of individual proteins. To do this, we developed a theory for the quantitative understanding of modulations in ionic current that arise from the rotational dynamics of single proteins as they move through the electric field inside the nanopore. The approach allows us to measure the five parameters simultaneously, and we show that they can be used to identify, characterize and quantify proteins and protein complexes with potential implications for structural biology, proteomics, biomarker detection and routine protein analysis.
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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.