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Site-directed mutagenesis analysis have shown that Lys11 and Lys90 are vital for the bioactivity of TNF-α[30, 31].
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Our recent site-directed mutagenesis analysis of VA387 has identified a number of additional amino acids around the carbohydrate binding interface that are also involved in HBGA binding [35].
Mutagenesis analysis of AtDME has revealed that the conserved DNA glycosylase domain and flanking domains A, and B, are necessary and sufficient for DME enzymatic activity [ 18].
Quantitative trait locus (QTL) analysis has revealed a polygenic control for leaf shape variation in different species suggesting that loci discovered by mutagenesis may only explain part of the naturally occurring variation in leaf shape.
Moreover, even if IS analysis has not been fully standardized yet, drug administration agencies require to perform IS analysis both in preclinical experimentations and GT clinical trials to identify potential insertional mutagenesis events.
The YPLAGR motif corresponds to the small α-helix-3 (α-3) on the crystal structure of vinorine synthase [ 42], but no mutagenesis analysis targeting this region has yet been conducted.
Mutagenesis analysis of G1064 and C1192 has shown that mutations at both sites are well tolerated and confer resistance to spectinomycin (66, 67).
Site-specific mutagenesis analysis of C. necator PHA synthase had shown that the conserved cystein-319, aspartate-480 and histidine-508 of the class I synthase are required for enzyme activity.
Further site-directed mutagenesis analysis revealed that His418 and Ser420 had little effect on metalloid binding while the C172A single mutant and C172A/H453A double mutant exhibited significantly decreased affinity for SbIII, suggesting that C172 is the third residue that participates in high-affinity binding.
A functional 4EHP-binding motif present in Prep1 has been also identified by mutagenesis analysis.
Here we have performed a complete in silico mutagenesis analysis to assess the functional essentiality of all possible nonnative point mutants in the entire hMC4R protein (332 residues).
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