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For visualization and manipulation of the 3D molecule, we used the spdbv 3.7 tool (http://swissmodel.expasy.org/spdbv/) [75].
To allow largely unrestricted relative motion of two A1 modules in the A1-A1 molecule, we used a flexible linker Gly-Ser-Ser-Gly to connect A1 modules.
Because Psn is known to process Notch into a signaling molecule, we used the same logic to judge the effectiveness of twelve UAS-Psni lines generated in our lab or collected from the Drosophila community (see Methods).
To test whether crosslinking of the one-armed YW211.31 antibody would restore the Wnt potentiation function of the whole IgG molecule, we used the HT-1080 celineine that exhibits autocrine Wnt and Wnt2-induced signaling potentiated by YW211.31.57 antibody (Figure 4E and 4F).
To purify this molecule, we used LePRK2 dephosphorylation as a tracking assay.
To generate a potential docked conformation of the entire molecule, we used the docking program 'Glide' from the Schrödinger software suite.
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However, as the protein files provided by the sc-PDB do not contain water molecules, we used the corresponding original files from the PDB instead.
To evaluate the neuroprotective activity of these molecules, we used midbrain cultures and various experimental conditions that promote dopaminergic cell loss.
The dot-dot distance, l, in these molecules is between 0.5 to 0.8 Å. Bistability and electron localizability of these molecules have been studied in [3, 46, 49]. Figure 4 Geometry of the molecules we used in our calculations.
To analyze the expression of cell surface molecules we used monospecific antibodies, fluorochrome dyes and flow cytometry.
To achieve a uniform expression of the transfected cDNA and to make sure that the transfected MHCII subunits are integrated into endogenous MHCII-Ii complexes and introduced into the biosynthetic route of MHCII molecules, we used stably transfected cell lines.
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