ArticlePeerJ2019
Heterologous expression, purification and biochemical characterization of a glutamate racemase (MurI) from
Article in PeerJ, 2019. 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, 3 citations in OpenAlex.
- L-serine-O-sulfate alters cellular ultrastructure and mitigates the capacity of biofilm formation inCurrent research in microbial sciences · 2025Article
- Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.Chemical Society reviews · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundGlutamate racemase (MurI) is a cofactor-independent enzyme that is essential to the bacterial peptidoglycan biosynthesis pathway and has therefore been considered an attractive target for the development of antimicrobial drugs. While in our previous study the essentiality of the
methodsStructure characterization prediction and multiple sequence alignment were performed by bioinformatic analysis. Recombinant His
resultsThe glutamate racemase gene from
conclusionThe findings of this study provide insight into the structure and biochemical traits of the glutamate racemase in
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Registered trials
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