Publications by authors named "O Mustafaev"
Background: RNA-seq has become a standard technology to quantify mRNA. The measured values usually vary by several orders of magnitude, and while the detection of differences at high values is statistically well grounded, the significance of the differences for rare mRNAs can be weakened by the presence of biological and technical noise.
Results: We have developed a method for cleaning RNA-seq data, which improves the detection of differentially expressed genes and specifically genes with low to moderate transcription.
Article Synopsis
- Researchers are developing new strategies to improve the production and purification of recombinant proteins in plants by optimizing gene codon composition and exploring regulatory sequences.
- A case study on interferon-αA demonstrated that using a thermostable protein stabilizer (lichenase) significantly enhances the yield of recombinant proteins without negatively affecting their biological activity.
- The combination of protein stabilization and methods for purifying fusion proteins leads to efficient and cost-effective approaches for producing valuable proteins in plant systems.
Clostridium thermocellum lichenase (endo-β-1,3;1,4-glucan-D-glycosyl hydrolase, EC 3.2.1.
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- Translation control plays a key role in how plants respond to environmental changes, highlighting the need to understand the gap between mRNA levels and their corresponding protein products.
- This review aims to outline experimental methods for studying differential translation in plants, summarize computational tools for assessing mRNA features related to translation efficiency, and verify these findings through experimentation.
- Additionally, it discusses future opportunities to identify specific structural characteristics of plant mRNAs that regulate differential translation through a combination of computational and experimental strategies.
A recombinant DNA in which the interferon αA (IFN-αA) gene sequence is integrated into a loop region of the gene coding thermostable lichenase was constructed. This approach of insertion fusion with thermostable lichenase is advantageous in terms of increasing the solubility, stability, and production of the fusion partner in soluble form in general and in the periplasm of bacterial cells in particular. Thus, the insertion of IFN-αA into the loop (53 a.
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