ArticleNature chemistry2021
Bottom-up fabrication of a proteasome-nanopore that unravels and processes single proteins.
Article in Nature chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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.
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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
65 citing papers in PubMed, 122 citations in OpenAlex.
- Article
- From DNA to full-length proteins through nanopore sequencing.Nature nanotechnology · 2026Article
- Exopeptidase-assisted nanopore peptide sequence identification.Nature communications · 2026Article
- Large-Diameter DNA-Scaffolded Nanopores Enabled by Loosely Packed Peptides for Single-Molecule Sensing.Angewandte Chemie (International ed. in English) · 2026Article
- Nanoarchitectonics of molecular machines, biomolecular machines, and microrobots in their collective behaviour.Chemical science · 2026Review
- High-resolution nanopore peptide sensing, profiling and sequence assembly.Nature nanotechnology · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Glycan Sequencing, A Brief Primer.Glycoscience & therapy · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Expression and Purification of CytK Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Protein abundance inference via expectation-maximization in fluorosequencing.Bioinformatics advances · 2026Article
- 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
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- Altered glycosylation of EVs in cancers: galectin-3-binding protein (LGALS3BP).Discover oncology · 2025Review
- Brownian motion data augmentation: a method to push neural network performance on nanopore sensors.Bioinformatics (Oxford, England) · 2025Article
- Controlled Sensing of User-Defined Aptamer-Based Targets Using Scanning Ionic Conductance Spectroscopy.ACS nano · 2025Article
- Nanopore-Functionalized Hybrid Lipid-Block Copolymer Membranes Allow Efficient Single-Molecule Sampling and Stable Sensing of Human Serum.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Redesign of Translocon EXP2 Nanopore for Detecting Peptide Fragments.Small methods · 2025Article
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
5 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The precise assembly and engineering of molecular machines capable of handling biomolecules play crucial roles in most single-molecule methods. In this work we use components from all three domains of life to fabricate an integrated multiprotein complex that controls the unfolding and threading of individual proteins across a nanopore. This 900 kDa multicomponent device was made in two steps. First, we designed a stable and low-noise β-barrel nanopore sensor by linking the transmembrane region of bacterial protective antigen to a mammalian proteasome activator. An archaeal 20S proteasome was then built into the artificial nanopore to control the unfolding and linearized transport of proteins across the nanopore. This multicomponent molecular machine opens the door to two approaches in single-molecule protein analysis, in which selected substrate proteins are unfolded, fed to into the proteasomal chamber and then addressed either as fragmented peptides or intact polypeptides.
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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.