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In order to confirm the function of SaSTT3A and SaSTT3B were truly conserved with their counterparts in the phylogenetic trees, we expressed them in A. thaliana stt3a-2 mutont tobserveve the phenotypic rescue.
Maize core oscillator genes are found to be largely conserved with their Arabidopsis counterparts.
Zebrafish OCRL1 and INPP5B are highly conserved with their human counterparts in terms of sequence identity and domain organization.
Although the core structural features of ligand engagement by viral Bcl-2 members are conserved with their mammalian counterparts, some intriguing differences exist.
Neurotransmitter-specific transporters (membrane and vesicular) and receptors (including G-protein coupled) are also highly conserved with their mammalian counterparts (Bargmann 1998).
In our study, several poplar phosphoproteins were highly conserved with their Arabidopsis ortholog(s), but their corresponding phosphorylation sites were not conserved (Additional file 9).
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Such positions may belong to the same orthologous functional elements (i.e. elements conserved in various genomes with respect to their function but not necessarily conserved with respect to their sequence) and could have important implications for viral fitness.
A picture is beginning to emerge for gene regulatory networks in sugar beet, in which genes homologous by sequence and protein function to their Arabidopsis counterparts are not necessarily conserved with respect to their developmental roles [ 5, 7].
Previous studies have revealed that the functions of rice Ehd2/RID1/OsID1 and maize ID1 are roughly conserved with respect to their role in flowering promotion and the tissue-specific expression of these genes, as there is high identity (82%) between their zinc finger domains (Matsubara et al. 2008; Park et al. 2008; Wu et al. 2008; Colasanti et al. 1998; Wong and Colasanti 2007).
Three peroxiredoxin protein sequences, YkuU (BPUM_1319), YgaF (BPUM_0826), and Tpx (BPUM_2581), are highly conserved with respect to their B. subtilis and B. licheniformis homologs (Table 3).
From the structures proposed, it is suggested that OsClpB-c, OsClpB-m and OsClpB-cyt proteins are remarkably conserved with respect to their predicted protein binding sites.
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