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The drug polymer interaction was validated by XRD studies, whereas the morphology and size characterization by SEM and zetasizer.
The interaction was validated by performing one to one protein-protein interaction between full length clones of OsMPK20-4 and OsMPK3.
This interaction was validated in vivo using coimmunoprecipitation (co-IP) both with endogenous proteins in MDCKII cells and exogenous TIAM1 in HEK293T cells.
This interaction was validated in three different cell lines (JEG3, HeLa, and LNCaP), thus proving its potential to be utilized in therapeutic treatment decision.
Protein interaction was validated by biochemical co-precipitation and confocal microscopy, followed by in situ proximity ligation assay microscopy to confirm close-range (<16 nm) interaction.
This interaction was validated in transfected mammalian cells and was also found to be conserved between PR8 and X-31 IAV strains.
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All combinations of fusion constructs scoring positive for an interaction were validated by repeating transformations and selection on dropout medium.
The proteins in each interaction were validated using KEGG pathways and the HPRD cancer signalling pathways.
The group of observed interactions was validated by several (mostly in silico) means and sources.
The specificity of these interactions was validated by comparison to wild-type brain eluates and elution with a scrambled peptide.
HO-2-adiponectin interactions were validated by the two-hybrid system assay.
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