To verify the specificity of fiber binding, we demonstrated that fiber molecules from the supernatants of Ad5-CRAD infected A549 cell cultures bound to CHO cells stably transfected with CAR cDNA, but not to the mock transfectants (Figure 3D).
To further ascertain the specificity of binding, we demonstrated that the formation of complexes C1 and C2 were inhibited by excess amounts of unlabeled NFY oligonucleotides but not with unlabeled non-specific Epstein-Barr nuclear antigen (EBNA) oligonucleotides.
Using RNA-protein binding assays, we demonstrate that basic amino acids 80 93 are required for high affinity binding of 28S rRNA and EBER-1 by L22.
By molecular modeling and binding experiments we demonstrated that MIBE binds to both receptors, while through functional assays we showed that MIBE inhibits the ERα- and GPER-mediated signaling.
In the MBs binding tests, we demonstrated that APT1 had a slightly higher binding capacity than APT2, which corresponds to the SPR results in terms of sensitivity of the functionalized sensor.
By analyzing single amino acid substitution mutants of the hZFP57 DNA binding domain we demonstrated that substitution of S244, G245 and R248, occupying position +2, +3 and +6 of ZF 3 α-helix and R276, located at position +6 of ZF4 helical region, have a dramatic effect on the interaction with DNA.
It is therefore likely that the binding we demonstrate here between mhttQ51 fibrils and TRiC, which thwarts the progression of fibers into sheaves, may involve mhttQ51 hydrophobic moieties that include the N17 domain.
By using a competitive binding assay, here we demonstrated that the technetium tricarbonyl indeed binds selectively to a His-tagged protein in the presence of a non-His-tagged protein and little or no (<2% ± 0.9%) non-specific labelling was observed.
Seven of the PU.1 mutations in AML patients affected the DNA-binding domain, and we demonstrated that those PU.1 mutations were deficient in DNA binding to and transactivation of the macrophage colony-stimulating factor receptor promoter, a direct PU.1 target gene.
We demonstrated that binding avidin to the biotin receptors on the self-assembled nanosensors causes a significant change in the network conductance that is dependent on the charge of the avidin protein.
Moreover, we demonstrated that binding to HDAC2-containing NuRD complex contributes to the nuclear localization of APPL1.
