ArticleJournal of visualized experiments : JoVE2014
Luminescence resonance energy transfer to study conformational changes in membrane proteins expressed in mammalian cells.
Article in Journal of visualized experiments : JoVE, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 14 citations in OpenAlex.
- Functional methods for evaluating the efficacy of retinal optogenetic therapy for vision restoration.Frontiers in neuroscience · 2026Review
- Isolation and characterization of extracellular vesicles and future directions in diagnosis and therapy.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2023Review
- Research progress of CRISPR-based biosensors and bioassays for molecular diagnosis.Frontiers in bioengineering and biotechnology · 2022Review
- Long-lived lanthanide emissionChemical science · 2021Article
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Stargazin Modulation of AMPA Receptors.Cell reports · 2016Article
- A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.The Journal of general physiology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Luminescence Resonance Energy Transfer, or LRET, is a powerful technique used to measure distances between two sites in proteins within the distance range of 10-100 Å. By measuring the distances under various ligated conditions, conformational changes of the protein can be easily assessed. With LRET, a lanthanide, most often chelated terbium, is used as the donor fluorophore, affording advantages such as a longer donor-only emission lifetime, the flexibility to use multiple acceptor fluorophores, and the opportunity to detect sensitized acceptor emission as an easy way to measure energy transfer without the risk of also detecting donor-only signal. Here, we describe a method to use LRET on membrane proteins expressed and assayed on the surface of intact mammalian cells. We introduce a protease cleavage site between the LRET fluorophore pair. After obtaining the original LRET signal, cleavage at that site removes the specific LRET signal from the protein of interest allowing us to quantitatively subtract the background signal that remains after cleavage. This method allows for more physiologically relevant measurements to be made without the need for purification of protein.
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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.