ArticleCell stress & chaperones2018
Heterologous expression of Oenococcus oeni sHSP20 confers temperature stress tolerance in Escherichia coli.
Article in Cell stress & chaperones, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- An integrative approach to improving the biocatalytic reactions of whole cells expressing recombinant enzymes.World journal of microbiology & biotechnology · 2021Review
- Engineering Lactococcus lactis as a multi-stress tolerant biosynthetic chassis by deleting the prophage-related fragment.Microbial cell factories · 2020Article
- Identification and Characterization of the Small Heat Shock Protein Hsp20 from Oenococcus oeni SD-2a.Current microbiology · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Small heat shock proteins (sHSPs) are heat shock proteins sized 12-43 kDa that can protect proteins from denaturation, particularly under high temperature; sHSPs thus increase the heat tolerance capability of an organisms enabling survival in adverse climates. sHSP20 is overexpressed in Oenococcus oeni in response to low temperatures. However, we found that overexpression of sHSP20 in Escherichia coli BL21 increased the microbial survival ratio at 50 °C by almost 2 h. Adding sHSP20 to the glutamate dehydrogenase solution significantly increased the stability of the enzyme at high temperature (especially at 60-70 °C), low pH values (especially below 6.0), and high concentration of metal ions of Ga
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