ArticleACS nano2019
Resolving Chemical Modifications to a Single Amino Acid within a Peptide Using a Biological Nanopore.
Article in ACS nano, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
42 citing papers in PubMed.
- Light-Driven, Phase-Locked Protein Pumping Through a Single Plasmonic Optofluidic Nanopore.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- High-resolution nanopore peptide sensing, profiling and sequence assembly.Nature nanotechnology · 2026Article
- Machine learning assisted single-molecule sensing towards standard-free quantification of per- and polyfluoroalkyl carboxylic acids.Nature communications · 2026Article
- Ionic species programmable synaptic plasticity in multimodal nanofluidic devices.National science review · 2026Article
- Engineering Linker-Enhanced OmpG Nanopores for Rapid Single-Molecule Protease Detection.Sensors (Basel, Switzerland) · 2025Article
- Insights to Resistive Pulse Sensing of Microparticle and Biological Cells on Microfluidic Chip.Biosensors · 2025Review
- Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.The Journal of membrane biology · 2025Review
- Single-molecule nanopore sensing of prolineChemical science · 2025Article
- Article
- Identification and Detection of a Peptide Biomarker and Its Enantiomer by Nanopore.ACS central science · 2024Article
- The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 2024Article
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Confirming Silent Translocation through Nanopores with Simultaneous Single-Molecule Fluorescence and Single-Channel Electrical Recordings.Analytical chemistry · 2023Article
- Multi-pass, single-molecule nanopore reading of long protein strands with single-amino acid sensitivity.bioRxiv : the preprint server for biology · 2023Article
- Review
- Nanopore discrimination and sensitive plasma detection of multiple natriuretic peptides: The representative biomarker of human heart failure.Biosensors & bioelectronics · 2023Article
- Article
- Nanopore-Based Fingerprint Immunoassay Based on Rolling Circle Amplification and DNA Fragmentation.ACS nano · 2023Article
- Nanopore Discrimination of Coagulation Biomarker Derivatives and Characterization of a Post-Translational Modification.ACS central science · 2023Article
- An Engineered OmpG Nanopore with Displayed Peptide Motifs for Single-Molecule Multiplex Protein Detection.Angewandte Chemie (International ed. in English) · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While DNA sequencing is now amply available, fast, and inexpensive, protein sequencing remains a tremendous challenge. Nanopores may allow for developing a protein sequencer with single-molecule capabilities. As identification of 20 different amino acids currently presents an unsurmountable challenge, fingerprinting schemes are pursued, in which only a subset of amino acids is labeled and detected. This requires modification of amino acids with chemical structures that generate a distinct nanopore ionic current signal. Here, we use a model peptide and the fragaceatoxin C nanopore to characterize six potential tags for a fingerprinting approach using nanopores. We find that labeled and unlabeled proteins can be clearly distinguished and that sensitive detection is obtained for labels with a spectrum of different physicochemical properties such as mass (427-1275 Da), geometry, charge, and hydrophobicity. Additionally, information about the position of the label along the peptide chain can be obtained from individual current-blockade event features. The results represent an important advance toward the development of a single-molecule protein-fingerprinting device with nanopores.
Indexed as
Identifiers
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.