ArticleACS nano2016
Semisynthetic Nanoreactor for Reversible Single-Molecule Covalent Chemistry.
Article in ACS nano, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 23 citations in OpenAlex.
- Understanding single-molecule reactions using nanopore-based techniques.Nature chemistry · 2025Review
- Medical and Nonmedical Applications of Synthetic Transmembrane Anion Transporters.Chemical reviews · 2025Review
- Programmable nano-reactors for stochastic sensing.Nature communications · 2021Article
- Use of an asparaginyl endopeptidase for chemo-enzymatic peptide and protein labeling.Chemical science · 2020Article
- Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings.Nature chemistry · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors.Nature communications · 2018Article
- DNA scaffolds support stable and uniform peptide nanopores.Nature nanotechnology · 2018Article
- Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization.ACS nano · 2017Article
- Single-molecule nanopore enzymology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore.ACS nano · 2017Article
- Engineering a pH responsive pore forming protein.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Protein engineering has been used to remodel pores for applications in biotechnology. For example, the heptameric α-hemolysin pore (αHL) has been engineered to form a nanoreactor to study covalent chemistry at the single-molecule level. Previous work has been confined largely to the chemistry of cysteine side chains or, in one instance, to an irreversible reaction of an unnatural amino acid side chain bearing a terminal alkyne. Here, we present four different αHL pores obtained by coupling either two or three fragments by native chemical ligation (NCL). The synthetic αHL monomers were folded and incorporated into heptameric pores. The functionality of the pores was validated by hemolysis assays and by single-channel current recording. By using NCL to introduce a ketone amino acid, the nanoreactor approach was extended to an investigation of reversible covalent chemistry on an unnatural side chain at the single-molecule level.
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What OpenQuestion 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 OpenQuestion graph.