ArticleMethodsX2021
Optimization of production of recombinant gamma-tubulin in bacteria.
Article in MethodsX, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 1 citations in OpenAlex.
- Secreted chimeric proteins as a strategy to correct SOX17 deficiency and attenuate the malignant phenotype of cholangiocarcinoma cells: a proof-of-concept study.Acta pharmacologica Sinica · 2026Article
- Targeting TUBG1 in RB1-negative tumors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Production of a protein of interest in bacteria and its purification from bacterial lysates are valuable tools for the purification of larger amounts of recombinant proteins. The low cost of culturing, and the rapid cell growth of bacteria make this host a good choice for protein production, but the folding and function of the purified protein might be altered due to the production of a eukaryotic protein in a prokaryotic host. Here, we provide a purification method for the purification of gamma (γ)-tubulin (TUBG) from soluble fractions of
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Registered trials
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