ArticleFrontiers in pharmacology2013
An Escherichia coli strain for expression of the connexin45 carboxyl terminus attached to the 4th transmembrane domain.
Article in Frontiers in pharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
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
7 citing papers in PubMed.
- Recombinant production of canine vitronectin for optimizing the culture of canine induced pluripotent stem cells.Regenerative therapy · 2025Article
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- An Efficient Method of Expression and Purification of Amyloid-Beta (AβMethods in molecular biology (Clifton, N.J.) · 2023Article
- Smoothing membrane protein structure determination by initial upstream stage improvements.Applied microbiology and biotechnology · 2019Review
- Secondary structural analysis of the carboxyl-terminal domain from different connexin isoforms.Biopolymers · 2016Article
- Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners.Biophysical journal · 2014Article
- Mind the gap! Connexins and pannexins in physiology, pharmacology and disease.Frontiers in pharmacology · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A major problem for structural characterization of membrane proteins, such as connexins, by nuclear magnetic resonance (NMR) occurs at the initial step of the process, the production of sufficient amounts of protein. This occurs because proteins must be expressed in minimal based media. Here, we describe an expression system for membrane proteins that significantly improves yield by addressing two common problems, cell toxicity caused by protein translation and codon bias between genomes. This work provides researchers with a cost-effective tool for NMR and other biophysical studies, to use when faced with little-to-no expression of eukaryotic membrane proteins in Escherichia coli expression systems.
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Registered trials
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