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Here we report that the CssB subunit of the CS6 protein confers a specific binding of this colonization factor to a glycosphingolipid present in human and rabbit small intestine.
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Populations of the Palearctic would represent the last outcomes of this colonization.
Past experimental data indicates that the MAH ΔGPL/4B2 mutant, which expresses a decreased ability to form biofilm on surfaces (Yamazaki et al., 2006a), and an impaired capacity to bind to human epithelial HEp-2 cells, also shows a decreased interaction with the intestinal tract of C. elegans, with deficiency in binding to and colonization of the epithelium.
On the other hand, the results of Hatakeyama et al. (2009) document SR proteins as carbohydrate-specific receptors, responsible for the sialyl LeX-dependent binding and lung colonization of B16 melanoma cells.
Thus, it appears that endothelial cells expressing cell surface SR splicing factors were responsible for the carbohydrate-dependent binding and lung colonization of the sialyl LeX-expressing B16-FTIII-M cells.
Using the rabbit non-ligated intestinal model (RITARD) it has been shown that CS6 mediates binding of ETEC in rabbit intestine, where colonization was obtained by a CS6-positive strain, but not with the isogenic CS6-deficient strain [11].
Two additional "presumptions" were also part of this traditional colonization scenario.
Following binding to, colonization of, and degradation of the MGL, invading microbes have been shown experimentally to have the potential to continue to influence the MGL and exert an effect on the host cells.
This colonization is the misrepresentation of yoga's intention, its many limbs, and its aims.
This colonization rate remained stable until 64 weeks of infection (Figure 1A B).
Return of SPI-19 to the ΔSPI-19 mutant, using VEX-Capture, complemented this colonization defect.
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