ArticleNano letters2019
Label-Free Detection of Post-translational Modifications with a Nanopore.
Article in Nano letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed.
- Site-specific post-translational modification detection by polar charged engineered MspA nanopores.Chemical science · 2026Article
- Epx4 Nanopore With Multiple Constrictions for Single-Molecule Identification.Small methods · 2026Article
- Nanopore-based massively parallel sensing for peptide profiling and protein identification.Nature communications · 2026Article
- Review
- Nanopore-Based Detection of Protein Posttranslational Modifications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Altered glycosylation of EVs in cancers: galectin-3-binding protein (LGALS3BP).Discover oncology · 2025Review
- Single-molecule nanopore sensing of prolineChemical science · 2025Article
- Redesign of Translocon EXP2 Nanopore for Detecting Peptide Fragments.Small methods · 2025Article
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
- Tracking flaviviral protease conformational dynamics by tuning single-molecule nanopore tweezers.Biophysical journal · 2025Article
- Direct Identification of O-Glycopeptides by Low-Temperature Assisted Nanopore Technique.Research (Washington, D.C.) · 2025Article
- Resolving Sulfation Posttranslational Modifications on a Peptide Hormone using Nanopores.ACS nano · 2024Article
- Location of Phosphorylation Sites within Long Polypeptide Chains by Binder-Assisted Nanopore Detection.Journal of the American Chemical Society · 2024Article
- Article
- Research Progress on Saccharide Molecule Detection Based on Nanopores.Sensors (Basel, Switzerland) · 2024Review
- Label-free electronic detection of peptide post-translational modification with functional enzyme-driven assay at the physical limit.Cell reports. Physical science · 2024Article
- Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Identification and Detection of a Peptide Biomarker and Its Enantiomer by Nanopore.ACS central science · 2024Article
- High-throughput assays to assess variant effects on disease.Disease models & mechanisms · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications (PTMs) of proteins play key roles in cellular processes. Hence, PTM identification is crucial for elucidating the mechanism of complex cellular processes and disease. Here we present a method for PTM detection at the single-molecule level using FraC biological nanopores. We focus on two major PTMs, phosphorylation and glycosylation, that mutually compete for protein modification sites, an important regulatory process that has been implicated in the pathogenic pathways of many diseases. We show that phosphorylated and glycosylated peptides can be clearly differentiated from nonmodified peptides by differences in the relative current blockade and dwell time in nanopore translocations. Furthermore, we show that these PTM modifications can be mutually differentiated, demonstrating the identification of phosphorylation and glycosylation in a label-free manner. The results represent an important step for the single-molecule, label-free identification of proteoforms, which have tremendous potential for disease diagnosis and cell biology.
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.