ArticlePloS one2011
Expression screening of fusion partners from an E. coli genome for soluble expression of recombinant proteins in a cell-free protein synthesis system.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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
8 citing papers in PubMed, 19 citations in OpenAlex.
- Development of a Chicken Immunoglobulin Heavy Chain Variable Region (VH) Single-Domain Antibody (sdAb) Against Calsequestrin (CSQ) and Its Application.Antibodies (Basel, Switzerland) · 2025Article
- Cell-free synthetic biology: Orchestrating the machinery for biomolecular engineering.Biotechnology notes (Amsterdam, Netherlands) · 2022Article
- Production of Recombinant Horseradish Peroxidase in an Engineered Cell-free Protein Synthesis System.Frontiers in bioengineering and biotechnology · 2021Article
- Surface patches on recombinant erythropoietin predict protein solubility: engineering proteins to minimise aggregation.BMC biotechnology · 2019Article
- Characterisation of a cell-free synthesised G-protein coupled receptor.Scientific reports · 2017Article
- An Efficient Genome-Wide Fusion Partner Screening System for Secretion of Recombinant Proteins in Yeast.Scientific reports · 2015Article
- Soluble expression of proteins correlates with a lack of positively-charged surface.Scientific reports · 2013Article
- Synthetic in vitro circuits.Current opinion in chemical biology · 2012Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While access to soluble recombinant proteins is essential for a number of proteome studies, preparation of purified functional proteins is often limited by the protein solubility. In this study, potent solubility-enhancing fusion partners were screened from the repertoire of endogenous E. coli proteins. Based on the presumed correlation between the intracellular abundance and folding efficiency of proteins, PCR-amplified ORFs of a series of highly abundant E. coli proteins were fused with aggregation-prone heterologous proteins and then directly expressed for quantitative estimation of the expression efficiency of soluble translation products. Through two-step screening procedures involving the expression of 552 fusion constructs targeted against a series of cytokine proteins, we were able to discover a number of endogenous E. coli proteins that dramatically enhanced the soluble expression of the target proteins. This strategy of cell-free expression screening can be extended to quantitative, global analysis of genomic resources for various purposes.
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