ArticleMethods in cell biology2017
Fluorescence polarization assays to measure interactions between Gα subunits of heterotrimeric G proteins and regulatory motifs.
Article in Methods in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 2 citations in OpenAlex.
- Other Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.Biomolecules · 2023Article
- Specific inhibition of GPCR-independent G protein signaling by a rationally engineered protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Fluorescence polarization (FP) is a simple and sensitive method allowing for the quantification of interactions between proteins and fluorescently tagged small molecules like peptides. Heterotrimeric G proteins are critical signal transducing molecules and their activity is controlled by a complex network of regulatory proteins. Some of these regulators have defined short motifs (<40 amino acids) that are sufficient to bind G proteins and subsequently modulate their activity. For these cases, FP represents a robust and quantitative method to characterize the G protein regulator interaction. Here we describe FP assays in a 384-well plate format to quantify interactions between Gα subunits of heterotrimeric G proteins and peptides corresponding to the Gα binding and activating (GBA) or GoLoco motifs, which are present in some proteins with guanine nucleotide exchange factor (GEF) (e.g., GIV/Girdin) or guanine nucleotide dissociation inhibitor (GDI) (e.g., RGS12) activity, respectively. This assay can be used to determine equilibrium dissociation constants, characterize the impact of single amino acid point mutations on the Gα-peptide interaction, and is suitable for high-throughput screening.
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