Sentence examples for binding studies suggest that from inspiring English sources

In vitro binding studies suggest that domain 1 and domain 4 from different beta subunits act together to bind the cytokine ligand [40], [41].

In contrast, these binding studies suggest that the di-ubiquitin molecule interacts with NEMO in an asymmetric fashion.

These binding studies suggest that JAZ ZF34 recognizes extended A-form helices independent of either sequence or the presence of local noncanonical structures.

Results of the peptide binding studies suggest that parent N sequences should interact functionally with HSP72 whereas mutant sequences should not.

Furthermore, the modeled interactions together with the mutant construct binding studies suggest that this conserved cleft is a site of favorable lipid interaction for both cholesterol and stearic acid.

In vitro binding studies suggest that parasite strains from asymptomatic controls with parasitaemia have high levels of CD36 binding, whereas strains from individuals with non-severe, uncomplicated disease have moderate levels of CD36 binding.

Fluorescence binding studies suggested that citral strongly binds to MARK4 and thereby inhibits its enzyme activity which was measured by the kinase inhibition assay.

Extensive direct binding studies suggested that erlotinib, gefitinib and lapatinib all bind similarly (within 3-fold) to both wild-type inactive and mutationally activated forms of EGFR-TKD [ 14].

P1 is located proximal to the binding site of HLA-DM and binding studies suggested that HLA-DM interacts specifically with the flexible empty hydrophobic P1-pocket [21].

Analysis of the APPL1 BAR-PH domain crystal structure together with in vitro binding studies suggests that APPL1 BAR-PH homodimers form heterotypic RAB5 binding platforms in which the BAR domain of one monomer and the PH domain of a second monomer interact with GTP-RAB5 on each end of the curved BAR-PH dimer [12].

Nevertheless, from the biophysical and structural perspective our results indicate that Diva is structurally suited to function as other negative regulators of cell death, in contrast to recent binding studies suggesting that the structure of Diva reveals a functionally divergent protein [22].