By examining the interaction term, we verified this hypothesis.
Based on the NMR analysis and our previous structures of IgFLNa17-GPIbα and IgFLNa21-integrin β7 complexes, we proposed a model for the interaction, and we verified it by introducing point mutations in both repeat 23 of full length FLNa and in FilGAP.
In this study, in order to further exploit tumor stoma interactions, we first verified whether tumor cells release soluble mediators able to fragment the S100A8 protein.
For GadE, C3NET predicted three interactions we could verify, one between gadE and gadB, one between gadE and hdeD and the third between gadE and yhiD.
In these curves without intersite interaction, we also find three regions verifying only one of the following affirmations: (1) the greater q, the greater χ and (2) the greater q, the lesser χ.
To further verify this interaction, we performed a titration experiment of zeta potential with GO concentration fixed at 5 μg/mL.
In our work, in addition to analyzing the use of interaction models and prototypes, we verified that it is possible to use it for UML diagrams.
To verify the C4BP M1 protein interaction, we carried out an additional TX-MS experiment using commercial C4BP.
To verify the in vitro interaction, we further performed endogenous immunoprecipication assay.
Then, we verified the interaction between p65 and SUMO2/3, and found TNF-α promoted their interaction.
We verified two interaction domains identified by an IVV experiment, including a globular domain in which the interaction region is clearly distinguished from the rest of the protein (Figure 2C).
