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We quantified the activity of PON1 towards paraoxon, determined two prominent genetic variants affecting PON1-activity, and assessed the consistency and proportionality of relationships between genotype, phenotype and risk of future CAD.
Using an adaptation of their methods, we performed electroporation with various green fluorescent protein (GFP) reporter constructs analogous to the previously described Nxnl1 and Nxnl2 luciferase constructs, and then quantified the activity of the promoter fragments by measuring the cellular fluorescence of the electroporated retinas.
We quantified the activity of caspase-3 by examining the proportion of cleaved-caspase-3 fragment (17 kDa) in the FL-caspase-3 (35 kDa).
To investigate whether apoptosis was triggered following Tv6 treatment, we quantified the activity of caspases 3 and 7 in treated and control cells.
We quantified the activity of three enzymes involved in plant defense in response to insect herbivores: peroxidase (POD), polyphenol oxidase (PPO) and lipoxygenase (LOX).
In a follow-up study, Porton et al. [ 29] quantified the activity of the enzyme telomerase in PBL and found a nominally significant decrease in telomerase activity in individuals with schizophrenia compared to unaffected individuals.
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To elucidate whether enzymatic antioxidants are responsible for the differing stress resistances and life expectancies observed in the Harpegnathos saltator groups, we quantified the activities of systems involved in ROS detoxification.
Here, we describe a rational mutagenesis scheme that deconvolves the function of four activation domain sequence features acidity, hydrophobicity, intrinsic disorder, and short linear motifs by quantifying the activity of thousands of variants in vivo and simulating their conformational ensembles using an all-atom Monte Carlo approach.
Because of the large number of deformation modes, each with limited deformation systems, a polycrystalline model is employed to identify and quantify the activity of each mode.
In the current contribution the reaction used to quantify the activity of the free enzyme, CLEAs, supernatant and washing solutions from CLEAs preparation, was the hydrolysis of triolein performed in an emulsioned system.
Here, we show that a 17-mer peptide corresponding to residues 187 203 of SNAP-25, which has earlier been shown to be a substrate for BoNT/A, can be used as a substrate for quantifying the activity of BoNT/C1(1 430).
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