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Studies in Dr. Shiff's laboratory have shown that aspirin and other anti-inflammatory drugs improve the efficiency of turnover in the cells lining the intestine, getting rid of cells with cancer-causing mutations before they take hold.
Turnover of dIno (a natural substrate for PNP) under similar reaction conditions revealed that the efficiency of turnover for dIno (16.6 min−1) was approximately 57-fold greater than that for 1, N-ε-dA (0.3 min−1).
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This makes it less likely that the heat-specific enhancement in polyadenylated transcripts is the consequence of a reduced efficiency of transcript turnover.
The degree of uncoupling can be quantified by measuring the endpoint biomass or methane yield and by determining the metabolic efficiency of substrate turnover.
As a main conclusion, Trp-377 appears responsible for the high-turnover catalytic site, since its substitution (W377S variant) completely prevented high-turnover oxidation of RB19 and DMP (and decreased over 40-fold the catalytic efficiency of high-turnover ABTS oxidation).
In most cases, however, what is hoped for is an efficiency in terms of turnover rates, yields, and stereoselectivities which is very close to that of the parent, non-dendritic analogous catalysts.
Furthermore, a quantum efficiency of 6.9% and turnover number of 2210 were achieved by the PEDOT-coated electrode.
Since RhoC interaction with PKN3 may facilitate nucleocytoplasmic shuttling [ 22, 40], one can hypothesize that after RhoC-mediated PKN3 translocation to the nucleus, arachidonic acid may interact with the kinase to increase the efficiency of substrate interaction and turnover.
Bulk electrolysis in the presence of cyclooctene yields cyclooctene oxide and shows that the best catalyst complexes (in terms of current efficiency and turnover) are based on ligands containing an ethano (Salen complexes) or a 1,2-cyclohexylidene (Salchx complexes) bridging unit and 5,5′-dichloro substituents.
Both the cell respiratory control ratio and mitochondrial coupling efficiency are bioenergetic parameters that reflect multiple processes underlying oxidative phosphorylation, including substrate oxidation, proton leak across the mitochondrial inner membrane, and, in case of coupling efficiency, ATP turnover [19,20].
Correspondingly, as a mechanism to limit material expenditure and increase efficiency, the turnover rates of many nerve terminal proteins are exceptionally slow relative to those of proteins in the nerve cell body or other cell types (Barber and LoPachin 2004; Barber et al. 2007; Calakos and Scheller 1996; Katyare and Shallom 1988; Lin and Scheller 2000).
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CEO of Professional Science Editing for Scientists @ prosciediting.com