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Here, we present the X-ray crystal structures of a dominant-negative form of human Scp1 (D96N mutant) bound to mono- and diphosphorylated peptides encompassing the CTD heptad repeat (Y1S2P3T4S5P6S7).
The N-terminal deletion mutant bound to ActRIIB in the co-immunoprecipitation assay, which increased with the addition of betaglycan (Figs. 4B and S8).
As shown in Figure 4D, Pc2 and the SIM1 deletion mutant bound to GST-SUMO1, whereas binding of the SIM2 or double SIM mutant was clearly reduced.
Inactive Rac1 mutant bound to the N-terminus of Abi1 (residues 1-186, Fig. 5B) whereas active Rac1 bound to the C-terminal Abi1 fragment containing exon 10 (residues 303-C-terminus, Fig. 5B).
As shown in Fig. 11B, neither NUP98-HOXA9 nor its N51S mutant bound to the HEY1 promoter, supporting the notion that its transactivation is independent of direct homeodomain-DNA interaction.
Proteins were eluted from the protein A coupled antibody column in a final volume of 40 µl. 10 µg of GST-TTC4 (wild type or mutant) bound to glutathione beads was incubated with 6 µg of HSP90 in 10 mM Tris pH 7.5, 150 mM NaCl, 0.1% triton X100 and protease inhibitors (complete EDTA free, Roche).
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According to ITC analysis (Supplementary Table S1 and Figure S5), the six mutants bound to Cc with slightly larger KD values than 14-3-3ε FL WT.
These mutants bound to both FADD and caspase-8, but could not block apoptosis or the formation of death effector filaments.
We have determined the three-dimensional structures of selected mutants bound to the substrate analogue nicotinic acid, using X-ray crystallography.
All pyrin mutants bound to PSTPIP1 and reticularized PSTPIP1 filaments in a manner similar to wildtype pyrin (Figure 6A R).
All three mutants bound to PG like the wild-type, and no significant differences in the binding affinity were observed.
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