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It is interesting that one of the β-hexosaminidase genes identified (Hex2_Ci) on the genome of the ascidian C. intestinalis has also conserved the size of several exons corresponding to vertebrate exons 2, 6, 7, 8,11, 12 and 13, consistent with this structure representing an ancestral chordate layout.
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And trading on our innate laziness, default settings have also conserved resources: when Rutgers University changed its printers' settings to double-sided, it saved more than seven million sheets of paper in one semester in 2007.
The three other characterized families of yCCR4-related proteins have also conserved catalytic residues and structural elements of the Mg2+-dependent nuclease core.
Although this domain has not been identified in CAG at the sequence level, there is experimental evidence for CAG binding to PCNA suggesting that besides CAG other pogo-related proteins might have also conserved this function (fig. 1 A).
The fact that the detailed structure of this domain (at the level of individual amino acids) has been conserved over evolution is often taken as an indication that its mechanism has also been conserved.
The discovery of a TID domain at the far C-terminus of nvp63 suggests the existence of a regulatory mechanism for nvp63 protein activity that has also been conserved through evolution.
Notably, this glutamine has also been conserved in Fam20A throughout evolution.
Expression of human K protein rescues these fly phenotypes, suggesting that like the structure, K protein function has also been evolutionarily conserved.
Beyond this, our approach has also detected large conserved genes such as CDS of 9 and 11 exons encoding an importin and an ATPase respectively (see Additional File 1).
Use of the C. elegans model has also delineated several conserved host pathways modulating infection outcomes, including the p38 mitogen-activated protein kinase (MAPK), TGF-β and DAF-2 insulin/IGF-1 signalling pathways (Kim et al., 2002; Mallo et al., 2002; Garsin et al., 2003).
A comparison of amino acid sequences and crystal structures of the heme-copper oxidases has also identified strictly conserved residues in the ligand channels of these enzymes, including that of Tt ba3, which may play important roles in modulating access of ligands to the binuclear active site.
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