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The nisin-controlled gene expression (NICE) system, which utilizes a nisin-inducible promoter to express downstream genes [ 21], is one of the most efficient expression systems and is commonly used with L. lactis and other LAB [ 22, 23].
To maximize the potential of industrial plants as a production system for proteins, efficient expression systems utilizing promoters that optimize transgene expression, 5′-untranslated region elements for efficient translation, and appropriate post-translational modifications and localization must be developed.
Currently there are no efficient expression systems available for recombinant production of hGAD65.
Efficient expression systems exist for antibody (Ab) molecules, which allow for characterization of large numbers of individual Ab variants.
Therefore a lot of efforts have focused on the development of efficient expression systems based on chromosomal integration of expression cassettes [ 10, 11].
Furthermore, the aspects described here are most probably also the main reason why host/vector systems using the phosphate starvation-inducible promoter phoA show high productivities, as they tend to be very efficient expression systems [ 9, 17].
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These results demonstrated that E. coli is a versatile and efficient expression system for multivalent trimerbody-based molecules that is suitable for their industrial production.
Our goal was to find a fast and efficient expression system for protein engineering and directed evolution studies of the two fungal enzymes.
Lacking of an efficient expression system that produces sufficient amounts of active and homogenous receptors hinders progress in the functional and structural characterization of the 5-HT2c receptor.
The ability of a series of vectors incorporating strong transcriptional and translational signals to provide an efficient expression system for hER-E/F was investigated.
This study reports the first efficient expression system enabling the production of a functional protein in O. oeni in enological conditions.
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