ArticleProtein science : a publication of the Protein Society2008
Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Modular Nanoparticle Platform for Solution-Phase Optical Sensing of Protein-Protein Interactions.ACS applied optical materials · 2025Article
- Ubiquitination detection techniques.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Article
- Assessing Protein Interactions for Clustering of Mitochondrial Urea Cycle Enzymes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Quantitative FRET (qFRET) Technology for the Determination of Protein-Protein Interaction Affinity in Solution.Molecules (Basel, Switzerland) · 2021Review
- MOLGENGO: Finding Novel Molecules with Desired Electronic Properties by Capitalizing on Their Global Optimization.ACS omega · 2021Article
- In Vitro Analytical Approaches to Study Plant Ligand-Receptor Interactions.Plant physiology · 2020Review
- Generation of a Quantitative Luciferase Reporter for Sox9 SUMOylation.International journal of molecular sciences · 2020Article
- UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor.Nature structural & molecular biology · 2019Article
- Protein-Protein Affinity Determination by Quantitative FRET Quenching.Scientific reports · 2019Article
- In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress.eLife · 2018Article
- Structural insights into enzymatic [4+2]Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Visualization of NO3⁻/NO2⁻ Dynamics in Living Cells by Fluorescence Resonance Energy Transfer (FRET) Imaging Employing a Rhizobial Two-component Regulatory System.The Journal of biological chemistry · 2016Article
- A new trend to determine biochemical parameters by quantitative FRET assays.Acta pharmacologica Sinica · 2015Review
- Article
- SUMO chain-induced dimerization activates RNF4.Molecular cell · 2014Article
- Article
- Development of a steady-state FRET-based assay to identify inhibitors of the Keap1-Nrf2 protein-protein interaction.Protein science : a publication of the Protein Society · 2013Article
- Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleus.The Journal of biological chemistry · 2013Article
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4 authors.
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Abstract
Protein-protein binding and signaling pathways are important fields of biomedical science. Here we report simple optical methods for the determination of the equilibrium binding constant K(d) of protein-protein interactions as well as quantitative studies of biochemical cascades. The techniques are based on steady-state and time-resolved fluorescence resonance energy transfer (FRET) between ECFP and Venus-YFP fused to proteins of the SUMO family. Using FRET has several advantages over conventional free-solution techniques such as isothermal titration calorimetry (ITC): Concentrations are determined accurately by absorbance, highly sensitive binding signals enable the analysis of small quantities, and assays are compatible with multi-well plate format. Most importantly, our FRET-based techniques enable us to measure the effect of other molecules on the binding of two proteins of interest, which is not straightforward with other approaches. These assays provide powerful tools for the study of competitive biochemical cascades and the extent to which drug candidates modify protein interactions.
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