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Restraints for docking were based on experimental data of the PPIL1-binding epitope of SKIP as mapped by peptide array analysis and SKIP-interacting residues as mapped by HSQC-NMR by [1].
Restraints for the docking run were generated based on experimental data of the PPIL1-binding epitope of SKIP as mapped by peptide array analysis and SKIP-interacting residues of PPIL1 as mapped by HSQC-NMR by [1].
These predictions were confirmed by peptide array analysis, showing direct binding of recombinant Nck SH2 to both pTyr and pTyr on TSAd.
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Elimination of Tyr did not affect TSAd's binding to Nck SH2 in 293T cells (Fig. 1f), as predicted by SMALI and shown in the peptide array analysis (Fig. 1b).
As both PKD1 and Hsp20 are strongly implicated in hypertrophic signaling [ 11, 13, 15], we decided to probe the functionality of the complex by using cell-permeable peptides, designed using the information gleaned from peptide array analysis, to disrupt the Hsp20-PKD1 interaction.
We used high density peptide array analysis to identify regions in TDP-43 that are bound by TDP-43 itself and designed candidate peptides that might be able to reduce TDP-43 aggregation.
The peptide array analysis revealed five peptides located within the first 99 amino acid residues of GAD65, which were recognized by the IgG of both patients before rituximab treatment was initiated (Fig. 5 A C and Fig. S1).
In order to map the PPIL1-interacting region of SKIP at single amino acid resolution, a peptide array analysis was performed.
To test the SMALI predictions, we carried out a peptide array analysis of 15-mer TSAd phosphotyrosine peptides spotted to a nitrocellulose membrane.
A peptide-array analysis confirmed that the entire CD22 gene was well represented in the β-lactamase-positive infectious phages, except two small regions of 7 residues each.
We successfully verified all sORFs detected by tiling array analysis using RT-PCR.
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