ReviewMolecules (Basel, Switzerland)2021
Quantitative FRET (qFRET) Technology for the Determination of Protein-Protein Interaction Affinity in Solution.
Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025Review
- pH-Induced Conformational Change of the Chromophore of the Large Stokes Shift Fluorescent Protein tKeima.Molecules (Basel, Switzerland) · 2025Article
- Structural and Interactional Analysis of the Flavonoid Pathway Proteins: Chalcone Synthase, Chalcone Isomerase and Chalcone Isomerase-like Protein.International journal of molecular sciences · 2024Article
- DG-Affinity: predicting antigen-antibody affinity with language models from sequences.BMC bioinformatics · 2023Article
- Article
- Recent Advances of Representative Optical Biosensors for Rapid and Sensitive Diagnostics of SARS-CoV-2.Biosensors · 2022Review
- CDNF Interacts with ER Chaperones and Requires UPR Sensors to Promote Neuronal Survival.International journal of molecular sciences · 2022Article
- Article
- How Far Are We from the Completion of the Human Protein Interactome Reconstruction?Biomolecules · 2022Article
- A dynamical view of protein-protein complexes: Studies by molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
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Authors and funding
4 authors.
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Abstract
Protein-protein interactions play pivotal roles in life, and the protein interaction affinity confers specific protein interaction events in physiology or pathology. Förster resonance energy transfer (FRET) has been widely used in biological and biomedical research to detect molecular interactions in vitro and in vivo. The FRET assay provides very high sensitivity and efficiency. Several attempts have been made to develop the FRET assay into a quantitative measurement for protein-protein interaction affinity in the past. However, the progress has been slow due to complicated procedures or because of challenges in differentiating the FRET signal from other direct emission signals from donor and receptor. This review focuses on recent developments of the quantitative FRET analysis and its application in the determination of protein-protein interaction affinity (
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