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By studying multiple aspects of the molecular evolution of CEP genes (orthology, selection pressure, IOPDs and gene trees), we can conclude that CEP genes have diversified in angiosperms, particularly in the Poaceae and Solanaceae plant families.
Therefore, this finding showed that CEP is a low methoxyl pectic polysaccharide, with an average molecular weight about 65,000 g/mol.
Time-on-stream experiments suggest that CeP(2.5) catalyst exhibited constant activity until 20 h after which a slight drop of conversion of lactic acid was noticed.
Finally, the results indicated that CEP presents strong antioxidant activities in vitro (DPPH, chelating ability and reducing power), and significantly inhibits lipid peroxidation and the formation of fluorescent advanced glycation end products in glucose-BSA system model.
In this paper, we evaluate the Complex Event Processing (CEP) approach applied to real-time Grid monitoring and argue that CEP enables us to achieve two goals, otherwise difficult to combine: real-time access to monitoring data and advanced query capabilities.
Several studies indicate that CEP peptides regulate plant root and shoot growth, and affect lateral root and root nodule development [ 6, 7, 9, 11].
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This diversification of CEP genes and peptides in angiosperms (and the further diversification observed within Solanaceae and Poaceae), and the association of CEP genes with angiosperm-specific development, suggests that CEPs have been integral to the evolution of novel traits within the angiosperm lineage.
Experimental results show that CEP-trained filters achieve higher image quality.
Experimental evidence has also shown that CEP-1 regulates hundreds of genes during normal growth and development as well as under genotoxic stresses, and many of these genes contain a CEP-1-binding site (Derry et al., 2007).
These findings imply that CEP-1 might bind and transcriptionally repress the expression of telomerase RNAs and thereby reduce the telomerase activity in order to maintain chromatin stability in C. elegans.
It is worth mentioning that CEP-1 is highly conserved in prokaryotes and eukaryotes, and human CEP-1 shares 100%% homology of a 9 amino acid span with P. gingivalis α-enolase [37].
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