ArticleScientific reports2017
Qualifying a eukaryotic cell-free system for fluorescence based GPCR analyses.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Eukaryotic cell-free protein synthesis: Chassis diversification, system engineering, and emerging applications.Synthetic and systems biotechnology · 2026Review
- Cell-free protein synthesis and vesicle systems for programmable therapeutic manufacturing and delivery.Journal of biological engineering · 2025Review
- Cell-free protein synthesis platforms for accelerating drug discovery.Biotechnology notes (Amsterdam, Netherlands) · 2025Review
- Engineering cell-free systems by chemoproteomic-assisted phenotypic screening.RSC chemical biology · 2024Article
- Rapid One-Step Capturing of Native, Cell-Free Synthesized and Membrane-Embedded GLP-1R.International journal of molecular sciences · 2023Article
- Oligomerization of the heteromeric γ-aminobutyric acid receptor GABAScientific reports · 2022Article
- Cell Engineering and Cultivation of Chinese Hamster Ovary Cells for the Development of Orthogonal Eukaryotic Cell-free Translation Systems.Frontiers in molecular biosciences · 2022Article
- The Pore-Forming Hemolysin BL Enterotoxin fromToxins · 2021Article
- Targeted esterase-induced dye (TED) loading supports direct calcium imaging in eukaryotic cell-free systems.RSC advances · 2021Article
- Cell-free synthesis of the hirudin variant 1 of the blood-sucking leech Hirudo medicinalis.Scientific reports · 2020Article
- Cell-Free Protein Synthesis: A Promising Option for Future Drug Development.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Mammalian cell-free protein expression promotes the functional characterization of the tripartite non-hemolytic enterotoxin from Bacillus cereus.Scientific reports · 2020Article
- Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems.Frontiers in pharmacology · 2019Article
- Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins.Frontiers in pharmacology · 2019Review
- Proteoliposome Engineering with Cell-Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018Article
- A panoramic view on GPCRs: the 1st Berlin Symposium for Interdisciplinary GPCR research.Naunyn-Schmiedeberg's archives of pharmacology · 2018Article
- Functional G-Protein-Coupled Receptor (GPCR) Synthesis: The Pharmacological Analysis of Human Histamine H1 Receptor (HRH1) Synthesized by a Wheat Germ Cell-Free Protein Synthesis System Combined with Asolectin Glycerosomes.Frontiers in pharmacology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins are key elements in cell-mediated processes. In particular, G protein-coupled receptors (GPCRs) have attracted increasing interest since they affect cellular signaling. Furthermore, mutations in GPCRs can cause acquired and inheritable diseases. Up to date, there still exist a number of GPCRs that has not been structurally and functionally analyzed due to difficulties in cell-based membrane protein production. A promising approach for membrane protein synthesis and analysis has emerged during the last years and is known as cell-free protein synthesis (CFPS). Here, we describe a simply portable method to synthesize GPCRs and analyze their ligand-binding properties without the requirement of additional supplements such as liposomes or nanodiscs. This method is based on eukaryotic cell lysates containing translocationally active endogenous endoplasmic reticulum-derived microsomes where the insertion of GPCRs into biologically active membranes is supported. In this study we present CFPS in combination with fast fluorescence-based screening methods to determine the localization, orientation and ligand-binding properties of the endothelin B (ET-B) receptor upon expression in an insect-based cell-free system. To determine the functionality of the cell-free synthesized ET-B receptor, we analyzed the binding of its ligand endothelin-1 (ET-1) in a qualitative fluorescence-based assay and in a quantitative radioligand binding assay.
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