ArticleBiochemistry2016
Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Vacuolar iron transporters mediate resistance to triadimefon in plant pathogenic fungi.Nature communications · 2026Article
- A Lactose-BasedChem & bio engineering · 2025Article
- Cell-free protein synthesis and vesicle systems for programmable therapeutic manufacturing and delivery.Journal of biological engineering · 2025Review
- Developing anACS synthetic biology · 2025Article
- Review
- Function Investigations and Applications of Membrane Proteins on Artificial Lipid Membranes.International journal of molecular sciences · 2023Review
- Cell-Free Expression of a Therapeutic Protein Serratiopeptidase.Molecules (Basel, Switzerland) · 2023Article
- Application of polymersomes in membrane protein study and drug discovery: Progress, strategies, and perspectives.Bioengineering & translational medicine · 2023Review
- What remains from living cells in bacterial lysate-based cell-free systems.Computational and structural biotechnology journal · 2023Review
- Cell-Free Synthesis and Electrophysiological Analysis of Multipass Voltage-Gated Ion Channels Tethered in Microsomal Membranes.Advances in biochemical engineering/biotechnology · 2023Article
- Applications of Cell-Free Synthesized Membrane Protein Precipitates.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cell-free synthetic biology: Orchestrating the machinery for biomolecular engineering.Biotechnology notes (Amsterdam, Netherlands) · 2022Article
- Genetically Engineered Cellular Membrane Vesicles as Tailorable Shells for Therapeutics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Cell-Free Protein Synthesis: A Promising Option for Future Drug Development.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- A User's Guide to Cell-Free Protein Synthesis.Methods and protocols · 2019Review
- Cell-Free and Yeast-Based Production of the Malarial Lactate Transporter, PfFNT, Delivers Comparable Yield and Protein Quality.Frontiers in pharmacology · 2019Article
- Protein Sequences Recapitulate Genetic Code Evolution.Computational and structural biotechnology journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Cell free protein synthesis (CFPS) has emerged as a promising methodology for protein expression. While polypeptide production is very reliable and efficient using CFPS, the correct cotranslational folding of membrane proteins during CFPS is still a challenge. In this contribution, we describe a two-step protocol in which the integral membrane protein is initially expressed by CFPS as a precipitate followed by an in vitro folding procedure using lipid vesicles for converting the protein precipitate to the correctly folded protein. We demonstrate the feasibility of using this approach for the K(+) channels KcsA and MVP and the amino acid transporter LeuT. We determine the crystal structure of the KcsA channel obtained by CFPS and in vitro folding to show the structural similarity to the cellular expressed KcsA channel and to establish the feasibility of using this two-step approach for membrane protein production for structural studies. Our studies show that the correct folding of these membrane proteins with complex topologies can take place in vitro without the involvement of the cellular machinery for membrane protein biogenesis. This indicates that the folding instructions for these complex membrane proteins are contained entirely within the protein sequence.
Indexed as
Identifiers
What OpenQuestion holds
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.