ReviewProtein and peptide letters2014
Characterization of protein unfolding with solid-state nanopores.
Review in Protein and peptide letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed.
- Heterogeneous Multilayer Nanopores via Chemically Tuned Dielectric Breakdown for Single-Molecule Sensing.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Geometric Confinement in Solid-State Nanopores Enables Single-Molecule Discrimination of Ferritin Subunits and Translocation Bias.Nano letters · 2026Article
- Selective and Controllable Trapping of Single Proteins in Nanopores Using Reversible Covalent Bonds.ACS nano · 2026Article
- P.O.R.E.: A Programmable Ohmic Research Engine for Low-Cost Solid-State Nanopore Fabrication.IEEE access : practical innovations, open solutions · 2026Article
- Chemical Composition and Backbone Modifications Define Deformability of Nucleic Acid Nanoparticles.ACS nano · 2025Article
- Detection of Ultra-Short KYCDE Peptides Using SiElectrophoresis · 2025Article
- Solid-State Nanopores for Biomolecular Analysis and Detection.Advances in biochemical engineering/biotechnology · 2024Review
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor.Sensors (Basel, Switzerland) · 2023Article
- Unlocking the Power of Nanopores: Recent Advances in Biosensing Applications and Analog Front-End.Biosensors · 2023Review
- Investigation of α-Synuclein and Amyloid-β(42)-E22Δ Oligomers Using SiN Nanopore Functionalized with L-Dopa.Chemistry, an Asian journal · 2022Article
- Cataloguing the proteome: Current developments in single-molecule protein sequencing.Biophysics reviews · 2022Review
- Nanopore Technology for the Application of Protein Detection.Nanomaterials (Basel, Switzerland) · 2021Review
- Tuning Protein Discrimination Through Altering the Sampling Interface Formed between the Analyte and the OmpG Nanopore.ACS sensors · 2021Article
- Application of Solid-State Nanopore in Protein Detection.International journal of molecular sciences · 2020Review
- Article
- Label-Free Detection of Post-translational Modifications with a Nanopore.Nano letters · 2019Article
- Fabrication and practical applications of molybdenum disulfide nanopores.Nature protocols · 2019Article
- Paving the way to single-molecule protein sequencing.Nature nanotechnology · 2018Review
- Dynamics of a Molecular Plug Docked onto a Solid-State Nanopore.The journal of physical chemistry letters · 2018Article
- Sensing Native Protein Solution Structures Using a Solid-state Nanopore: Unraveling the States of VEGF.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
In this work, we review the process of protein unfolding characterized by a solid-state nanopore based device. The occupied or excluded volume of a protein molecule in a nanopore depends on the protein's conformation or shape. A folded protein has a larger excluded volume in a nanopore thus it blocks more ionic current flow than its unfolded form and produces a greater current blockage amplitude. The time duration a protein stays in a pore also depends on the protein's folding state. We use Bovine Serum Albumin (BSA) as a model protein to discuss this current blockage amplitude and the time duration associated with the protein unfolding process. BSA molecules were measured in folded, partially unfolded, and completely unfolded conformations in solid-state nanopores. We discuss experimental results, data analysis, and theoretical considerations of BSA protein unfolding measured with silicon nitride nanopores. We show this nanopore method is capable of characterizing a protein's unfolding process at single molecule level. Problems and future studies in characterization of protein unfolding using a solid-state nanopore device will also be discussed.
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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.