ArticleMethods in enzymology2013
Homogeneous time-resolved fluorescence assay to probe folded G protein-coupled receptors.
Article in Methods in enzymology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
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Who cites it
2 citing papers in PubMed.
- Anisotropic metal growth on phospholipid nanodiscs via lipid bilayer expansion.Scientific reports · 2016Article
- Fluorescence spectroscopy of rhodopsins: insights and approaches.Biochimica et biophysica acta · 2014Review
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Authors and funding
3 authors.
Funding
Abstract
Continued advances in G protein-coupled receptor (GPCR) structural biology and biochemistry depend in part on strategies to stabilize these polytopic membrane proteins in purified systems. New methods to measure properly folded GPCRs are needed to facilitate the identification of suitable conditions and ensure sample quality. Most GPCRs do not contain an intrinsic reporter on their functionality, so probes must be introduced. Here, we describe a fluorescence-based approach to quantitatively measure the chemokine receptor CCR5 with labeled antibodies. The assay is exceptionally sensitive and high-throughput. We detail procedures to label antibodies, characterize the system, and process data. We also describe several useful applications, including optimization of incorporation into nanoscale apolipoprotein bound bilayers (NABBs or nanodiscs), measurement of receptor stability, and competition binding assays.
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Registered trials
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