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In particular, the well-documented D380A variant, which lacks calcium, forms large circular fibrils.
This variant, which lacks exon 7 (encoding part of the zinc finger region), may have an important function in the testis, and its presence warrants further investigation.
In our present study, we have referred CTIP2 with all the 4 exons as CTIP2 long (CTIP2L), the variant lacking exon3 which is the actual CTIP2 as CTIP2 (Fig. 3A), and the variant which lacks both Exon2 and 3 as CTIP2 short (not shown).
The exception to this is the previously reported (Nogueira et al., 2007) 5′ VDS variant which lacks Exon 3 in its entirety.
(C ) The N44A variant, which lacks the hydrogen bond donor, is unable to form this hydrogen bond, thus destabilising the intermediate state and inhibiting the release of the product.
A single-nucleotide polymorphism (SNP), a C-to-T transition at position 1630 in the 3′UTR (rs6917) creates a variant, which lacks antiproliferative activity (Jupe et al, 1996b) and significantly reduces cell motility (Manjeshwar et al, 2004).
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By screening known coding-change polymorphisms for function, we were able to perform a directed genetic association study largely focused on this functional variant and including another nearby coding-change variant which lacked functional significance in our assays for comparison.
We were unable to express PAPP-A variants which lack the PA-LG module, suggesting a possible role in stabilization of the proteolytic domain.
EngD variants, which lack Trp162, showed a significant reduction in activity and an alteration in the distribution of cellohexaose degradation products, suggesting that Trp162 plays a direct role in substrate binding.
In reviewing the available literature, we recognized that previous reports had identified mutated eEF-2 variants which lack diphthamide but retain some degree of normal function in translation.
This study also provides evidence that RIG-I binds dsRNA devoid of free 5' tri-phosphate ends, and that poly-I/C is not a simple analog of dsRNA; i.e., poly-I/C has the unique ability to stimulate the helicase ATPase of RIG-I variants which lack the C-terminal regulatory domain.
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