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The differential expression of calmodulin and calmodulin binding proteins indicated that calcium may play a role in fiber initiation.
The unequal distribution of Ca+2 among ovule epidermal cells and the differential regulation of calmodulin and calmodulin binding proteins indicated that calmodulin mediated signaling could play an important role in fiber initiation and elongation.
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The uterine tissue compartments expressed different profiles of IGF-binding proteins, indicating that IGF bioavailability and bioactivity is differentially regulated throughout the regenerating endometrium.
Moreover, mammalian genomes encode several types of sPLA2-binding proteins, indicating that sPLA2 may have enzyme-independent activities related to the binding for specific sPLA2 receptor on the target cells [ 3].
Moreover, mammalian genomes encode several types of sPLA2-binding proteins, indicating that sPLA2s may have enzyme-independent activities related to their ability to bind to cellular target proteins [ 3].
Our phylogenetic tree separates these two groups into distinct clusters; however, the groups are clearly evolutionarily related compared with other calcium-binding proteins, indicating that there may have been relatively rapid diversification of these proteins in the time since ctenophores and cnidarians diverged.
The size of the PBP-βL domain varies from about 200 amino acids in class D β-lactamases to over 400 amino acids in class C low molecular weight penicillin-binding proteins, indicating that the PBP-βL domain has undergone extensive diversification through modification of local structural elements [ 1- 5].
Structural analysis of Siah and Siah-interacting/calcyclin-binding protein indicates that calcyclin-binding protein is a component of an E3 ligase complex and that it is required to recruit an E2-substrate complex for the final step of ubiquitin transfer [ 47].
At 4 months of age 16% of the children in the study area had low levels of retinol binding protein indicating VAD [ 26], and that figure was 9% when controlled for CRP [ 26].
Ex vivo studies with F-amidine and Cl-amidine, using a cell line and an assay measuring PAD4-mediated citrullination of a nuclear protein and the resulting enhancement in binding to another protein, indicated that these inhibitors are bioavailable [ 59, 60].
The finding that SGTP competes with GTP in binding multiple heterotrimeric G proteins indicates that SGTP may affect heterotrimeric G-protein-mediated signaling.
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