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The mechanism associated with the positive p53 staining (protein binding to wild type p53 versus mutation of the p53 gene) was not determined.
While dasatinib binding to wild type Abl clearly influenced Abl conformation, no binding was detected between dasatinib and T315I.
The compounds of the library were further evaluated for their capability to compete with T4 for binding to wild type TTR by a gel filtration procedure [55] [57].
Data are reported in Fig. 6, and show that binding to wild type CHO-K1 cells was greatly enhanced for CXCL12γ compared to CXCL12α.
Differences in e20 binding to wild type H77 and to each mutant were determined by FACS, following the protocol described above.
In contrast to what was observed for dasatinib binding to wild type Abl, when dasatinib was incubated at the same molar ratio with the T315I mutant, no major changes in HX were detected.
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The spatial separation of p85α homodimerization from p110α interaction sites is further supported by our observations that a truncation p85α mutant, A360*, which lacks the nSH2-iSH2-cSH2 fragment to bind p110α, displayed comparable p85α homodimerization and PTEN binding to wild-type (WT) p85α.
The method exploits affinity data for a series of organic chemical compounds binding to wild-type and artificially mutated receptors.
In the 1H-15N Hspectracomparedmpared with that of free PHD1KDM5B, the binding to wild-type H3A1 (i.e., H3K4me0) produces a large shift in most of the cross-peaks of PHD1KDM5B, whereas the binding of the H3G1 variant does not induce this shift.
Furthermore, despite clear IgE binding to wild-type plant food extracts, lack of clinical symptoms in the hymenoptera venom-allergic group was not accompanied by high sIgG4 levels.
This mutation lies next to the K531 residue (shown in purple in Fig. 7a) that has been shown to confer heparin binding to wild-type AAV6 [35].
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