ArticleApplied and environmental microbiology2017
Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.
Article in Applied and environmental microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 49 citations in OpenAlex.
- Biochemical and structural characterization of AmyY fromApplied and environmental microbiology · 2026Article
- Molecular adaptations and engineering of extremophiles for synthetic biology and biotechnological applications.Frontiers in microbiology · 2026Review
- Molecular Evolution and Adaptation Strategies in Marine Ciliates: An Inspiration for Cold-Adapted Enzyme Engineering and Drug Binding Analysis.Marine drugs · 2024Review
- Challenges and prospects of microbial α-amylases for industrial application: a review.World journal of microbiology & biotechnology · 2023Review
- Biochemical Properties of a Cold-Active Chitinase from MarineMarine drugs · 2023Article
- Improving the catalytic activity of a detergent-compatible serine protease by rational design.Microbial biotechnology · 2023Article
- An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic CiliateMarine drugs · 2021Article
- Article
- Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties.Scientific reports · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The α-amylases are endo-acting enzymes that hydrolyze starch by randomly cleaving the 1,4-α-d-glucosidic linkages between the adjacent glucose units in a linear amylose chain. They have significant advantages in a wide range of applications, particularly in the food industry. The eukaryotic α-amylase isolated from the Antarctic ciliated protozoon
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.