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SAA contributed to the programming of the GridCell simulator and its graphical user interface.
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SAA synthesized the PEG-albumin and contributed to the manuscript.
Although we cannot completely rule out the possibility that β1 contributed to the increase in cholesterol efflux observed for S-HDL-SAA, its presence did not improve the efflux activity for HDL.
First, Saa1/2 −/− mice exhibit increased susceptibility to chemically-induced colitis in mice (Eckhardt et al., 2010), suggesting that SAAs contribute to intestinal immunity.
Interestingly, mutations of CIAS1 cause several autoimmune inflammatory syndromes [ 39, 40] and its downregulation in SAA patients may contribute to the immunpathology of AA by augmentation of proinflammatory signals.
An amino acid mutation, an environmental factor, a proteolytic cleavage event or certain pathogenic intrinsic properties in the presence of high concentrations of SAA are then thought to contribute to the abnormal process of folding [ 8].
Nevertheless, current research has revealed new aspects in the pathophysiology of SAA: (a) telomere length correlates with the rate of relapse, clonal evolution and overall survival and (b) increased Th17 cell number contributes to the pathophysiology of SAA.
A number of these mechanisms could contribute to the effect on the SAA response and also on the difference in SAA response between the first and second vaccinations.
Results were poorest at low SAA concentrations, and in this range the high imprecision could contribute to the inaccurate results.
We sought to determine whether SAA would enhance the survival of DC during serum starvation and could then contribute to the development of a glucocorticoid-resistant phenotype in CD4+ T cells.
Failure to limit bacterial load at the intestinal epithelium increases the risk for inflammatory bowel disease, and since SAA might contribute to clearance of E. coli from the epithelium, we hypothesized that lack of SAA would increase the susceptibility to experimental colitis.
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