ArticleNature nanotechnology2013
Multistep protein unfolding during nanopore translocation.
Article in Nature nanotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 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
114 citing papers in PubMed, 307 citations in OpenAlex.
- Discriminating single-amino acid differences and post-translational modifications in negatively charged peptides with α-hemolysin nanopores.Journal of nanobiotechnology · 2026Article
- High-Rate Fingerprinting of Protein Isoforms by Quasi-regulated Enzyme-free Transport Through CytK Nanopores.Research square · 2026Article
- Review
- Regulation of Protein Transport in Functionalized PET Nanopores.The journal of physical chemistry. B · 2025Article
- Nanopore sensing of protein and peptide conformation for point-of-care applications.Nature communications · 2025Review
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
- Location of Phosphorylation Sites within Long Polypeptide Chains by Binder-Assisted Nanopore Detection.Journal of the American Chemical Society · 2024Article
- Translocation of linearized full-length proteins through an engineered nanopore under opposing electrophoretic force.Nature biotechnology · 2024Article
- Electro-osmotic Flow Generation via a Sticky Ion Action.ACS nano · 2024Article
- Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Molecular Determinants of Current Blockade Produced by Peptide Transport Through a Nanopore.ACS nanoscience Au · 2024Review
- Peptide sequencing based on host-guest interaction-assisted nanopore sensing.Nature methods · 2024Article
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor.Sensors (Basel, Switzerland) · 2023Article
- Electro-Osmotic Flow Generation via a Sticky Ion Action.bioRxiv : the preprint server for biology · 2023Article
- Enzyme-less nanopore detection of post-translational modifications within long polypeptides.Nature nanotechnology · 2023Article
- Review
- Unidirectional single-file transport of full-length proteins through a nanopore.Nature biotechnology · 2023Article
- Nanopore sensing reveals a preferential pathway for the co-translocational unfolding of a conjugative relaxase-DNA complex.Nucleic acids research · 2023Article
- Article
54 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 at 1 institution in 1 country.
Funding
Abstract
Cells are divided into compartments and separated from the environment by lipid bilayer membranes. Essential molecules are transported back and forth across the membranes. We have investigated how folded proteins use narrow transmembrane pores to move between compartments. During this process, the proteins must unfold. To examine co-translocational unfolding of individual molecules, we tagged protein substrates with oligonucleotides to enable potential-driven unidirectional movement through a model protein nanopore, a process that differs fundamentally from extension during force spectroscopy measurements. Our findings support a four-step translocation mechanism for model thioredoxin substrates. First, the DNA tag is captured by the pore. Second, the oligonucleotide is pulled through the pore, causing local unfolding of the C terminus of the thioredoxin adjacent to the pore entrance. Third, the remainder of the protein unfolds spontaneously. Finally, the unfolded polypeptide diffuses through the pore into the recipient compartment. The unfolding pathway elucidated here differs from those revealed by denaturation experiments in solution, for which two-state mechanisms have been proposed.
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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.