ReviewActa pharmacologica Sinica2015
A new trend to determine biochemical parameters by quantitative FRET assays.
Review in Acta pharmacologica Sinica, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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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Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Intracellular Retinoid-Binding Proteins (CRBP, CRALBP, CRABP) as Emerging Drug Targets in Retinal Disease.International journal of molecular sciences · 2026Review
- Let the peptides shine: SOX (Sulfonamido-OXine)-labelled peptides for direct kinase and phosphatase monitoring.RSC chemical biology · 2026Review
- Development of an EPR-based methodology to study protein-lipid interaction.Biophysical chemistry · 2026Article
- Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025Review
- Differential scanning fluorimetry followed by microscale thermophoresis and/or isothermal titration calorimetry as an efficient tool for ligand screening.Biophysical reviews · 2025Review
- Evaluation of High-Affinity Monoclonal Antibodies and Antibody-Drug Conjugates by Homogenous Time-Resolved FRET.ACS medicinal chemistry letters · 2024Article
- Evaluation of High-Affinity Monoclonal Antibodies and Antibody-Drug Conjugates by Homogenous Time-Resolved FRET.bioRxiv : the preprint server for biology · 2024Article
- Article
- Specific FRET Probes Sensitive to Chitosan-Based Polymeric Micelles Formation, Drug-Loading, and Fine Structural Features.Polymers · 2024Article
- A FRET-Based Assay for the Identification of PCNA Inhibitors.International journal of molecular sciences · 2023Article
- Article
- Live imaging of apoptotic signaling flow using tunable combinatorial FRET-based bioprobes for cell population analysis of caspase cascades.Scientific reports · 2022Article
- Determining translocation orientations of nucleic acid helicases.Methods (San Diego, Calif.) · 2022Review
- Quantitative FRET (qFRET) Technology for the Determination of Protein-Protein Interaction Affinity in Solution.Molecules (Basel, Switzerland) · 2021Review
- Probing ion channel macromolecular interactions using fluorescence resonance energy transfer.Methods in enzymology · 2021Article
- Evaluation of Caspase-3 Activity During Apoptosis with Fluorescence Lifetime-Based Cytometry Measurements and Phasor Analyses.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells.ACS omega · 2020Article
- An in vitro Förster resonance energy transfer-based high-throughput screening assay identifies inhibitors of SUMOylation E2 Ubc9.Acta pharmacologica Sinica · 2020Article
- Advanced FRET normalization allows quantitative analysis of protein interactions including stoichiometries and relative affinities in living cells.Scientific reports · 2019Article
- Protein-Protein Affinity Determination by Quantitative FRET Quenching.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Förster resonance energy transfer (FRET) has been widely used in biological and biomedical research because it can determine molecule or particle interactions within a range of 1-10 nm. The sensitivity and efficiency of FRET strongly depend on the distance between the FRET donor and acceptor. Historically, FRET assays have been used to quantitatively deduce molecular distances. However, another major potential application of the FRET assay has not been fully exploited, that is, the use of FRET signals to quantitatively describe molecular interactive events. In this review, we discuss the use of quantitative FRET assays for the determination of biochemical parameters, such as the protein interaction dissociation constant (K(d)), enzymatic velocity (k(cat)) and K(m). We also describe fluorescent microscopy-based quantitative FRET assays for protein interaction affinity determination in cells as well as fluorimeter-based quantitative FRET assays for protein interaction and enzymatic parameter determination in solution.
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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.