ArticleStructural dynamics (Melville, N.Y.)2019
Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability.
Article in Structural dynamics (Melville, N.Y.), 2019. 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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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Hydrophobic interactions determine the optimum temperature of a housekeeping enzyme.The Journal of biological chemistry · 2026Article
- A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- Improving the Thermostability and Activity of Transaminase FromFrontiers in chemistry · 2021Article
- CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacteriumComputational and structural biotechnology journal · 2021Article
- Extremophile - An Adaptive Strategy for Extreme Conditions and Applications.Current genomics · 2020Review
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
Protein thermal stability is an important field since thermally stable proteins are desirable in many academic and industrial settings. Information on protein thermal stabilization can be obtained by comparing homologous proteins from organisms living at distinct temperatures. Here, we report structural and mutational analyses of adenylate kinases (AKs) from psychrophilic
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