ArticleNature biotechnology2018
Real-time measurement of protein-protein interactions at single-molecule resolution using a biological nanopore.
Article in Nature biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 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
79 citing papers in PubMed.
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- Discriminating single-amino acid differences and post-translational modifications in negatively charged peptides with α-hemolysin nanopores.Journal of nanobiotechnology · 2026Article
- Engineering a Biological Nanopore for Monitoring Protein Dynamics and Conformational Changes at the Single-Molecule Level.ACS nano · 2026Article
- Biosensing With Nanofluidics.Exploration (Beijing, China) · 2026Review
- Dual-channel graph learning reveals similarity and complementarity in protein-protein interaction networks.PLoS computational biology · 2026Article
- Scalable Production of DNA-Probe-Functionalized Heteromeric MspA Nanopores for Biosensing.ACS applied materials & interfaces · 2026Article
- Catalytic Proximal Protein Oligomerization as an Anti-Tumor Strategy Targeting WDR5.Nature communications · 2026Article
- Review
- Real-Time Binding Kinetics of Membrane Protein-Protein Interactions in a Membraneless Setting.Analytical chemistry · 2025Article
- Protein Design Meets Single-Molecule Detection: Towards Programmable Nanopore Sensors.International journal of molecular sciences · 2025Review
- Fabrication of cytotoxic mirror image nanopores.Nature communications · 2025Article
- Hub Occupancy by Competitively Interacting Proteins Obeys a Simple Queuing Law.The journal of physical chemistry. B · 2025Article
- Article
- Quantum relaxometry for detecting biomolecular interactions with single NV centers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- MESM: integrating multi-source data for high-accuracy protein-protein interactions prediction through multimodal language models.BMC biology · 2025Article
- Regulation of Protein Transport in Functionalized PET Nanopores.The journal of physical chemistry. B · 2025Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- Localized topological states beyond Fano resonances via counter-propagating wave mode conversion in piezoelectric microelectromechanical devices.Nature communications · 2024Article
- Single-molecule evidence of Entropic Pulling by Hsp70 chaperones.Nature communications · 2024Article
19 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
2 authors.
Funding
Abstract
Protein-protein interactions (PPIs) are essential for many cellular processes. However, transient PPIs are difficult to measure at high throughput or in complex biological fluids using existing methods. We engineered a genetically encoded sensor for real-time sampling of transient PPIs at single-molecule resolution. Our sensor comprises a truncated outer membrane protein pore, a flexible tether, a protein receptor and a peptide adaptor. When a protein ligand present in solution binds to the receptor, reversible capture and release events of the receptor can be measured as current transitions between two open substates of the pore. Notably, the binding and release of the receptor by a protein ligand can be unambiguously discriminated in a complex sample containing fetal bovine serum. Our selective nanopore sensor could be applied for single-molecule protein detection, could form the basis for a nanoproteomics platform or might be adapted to build tools for protein profiling and biomarker discovery.
Identifiers
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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.