ReviewExtremophiles : life under extreme conditions2014
Thermal adaptation of α-amylases: a review.
Review in Extremophiles : life under extreme conditions, 2014. 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
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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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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
9 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular regulation by HBMC plant biology · 2024Article
- Structural and functional adaptation in extremophilic microbial α-amylases.Biophysical reviews · 2022Review
- Bioprospecting of microbial enzymes: current trends in industry and healthcare.Applied microbiology and biotechnology · 2022Review
- Glutamate Dehydrogenase (GdhA) of Streptococcus pneumoniae Is Required for High Temperature Adaptation.Infection and immunity · 2021Article
- Brewing with Starchy Adjuncts: Its Influence on the Sensory and Nutritional Properties of Beer.Foods (Basel, Switzerland) · 2021Review
- CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacteriumComputational and structural biotechnology journal · 2021Article
- Expression of3 Biotech · 2019Article
- Article
- Molecular Cloning and Characterization of a NovelBioMed research international · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The temperature adaptation of α-amylase can be gained by different adjustments in protein structure with consecutive effects on the stability and flexibility of the protein. In this review, meso, thermo and cold-active α-amylases have been compared with respect to their structure and intramolecular interactions. With decrease in temperature, the number of ionic interactions also decreases, leading to greater flexibility of proteins. It has also been observed that the proline and arginine content is higher in thermophilic amylases as compared to meso and psychrophilic amylases, increasing the rigidity and structural stability of protein molecule.
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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.