ArticleAnalytical chemistry2020
Nanomolar Protein-Protein Interaction Monitoring with a Label-Free Protein-Probe Technique.
Article in Analytical chemistry, 2020. 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, 20 citations in OpenAlex.
- Label-free technique for universal and sequence independent detection of oligonucleotides and nuclease activity.Nucleic acids research · 2025Article
- Out-of-sync evolutionary patterns and mutual interplay of major and minor capsid proteins in norovirus GII.2.The Journal of general virology · 2024Article
- Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024Review
- Luminescence-Based Techniques for KRAS Thermal Stability Monitoring.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Nanomolar Protein Thermal Profiling with Modified Cyanine Dyes.Analytical chemistry · 2023Article
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Targeting Protein-Protein Interfaces with Peptides: The Contribution of Chemical Combinatorial Peptide Library Approaches.International journal of molecular sciences · 2023Review
- Thermal Shift Assay for Small GTPase Stability Screening: Evaluation and Suitability.International journal of molecular sciences · 2022Article
- Rapid high-throughput compatible label-free virus particle quantification method based on time-resolved luminescence.Analytical and bioanalytical chemistry · 2022Article
- Myostatin and its Regulation: A Comprehensive Review of Myostatin Inhibiting Strategies.Frontiers in physiology · 2022Review
- Protease Substrate-Independent Universal Assay for Monitoring Digestion of Native Unmodified Proteins.International journal of molecular sciences · 2021Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein-protein interactions (PPIs) are an essential part of correct cellular functionality, making them increasingly interesting drug targets. While Förster resonance energy transfer-based methods have traditionally been widely used for PPI studies, label-free techniques have recently drawn significant attention. These methods are ideal for studying PPIs, most importantly as there is no need for labeling of either interaction partner, reducing potential interferences and overall costs. Already, several different label-free methods are available, such as differential scanning calorimetry and surface plasmon resonance, but these biophysical methods suffer from low to medium throughput, which reduces suitability for high-throughput screening (HTS) of PPI inhibitors. Differential scanning fluorimetry, utilizing external fluorescent probes, is an HTS compatible technique, but high protein concentration is needed for experiments. To improve the current concepts, we have developed a method based on time-resolved luminescence, enabling PPI monitoring even at low nanomolar protein concentrations. This method, called the protein probe technique, is based on a peptide conjugated with Eu
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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.