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Since F1-40 is used in this sensitive ELISA, molecular characterization and a detailed understanding of its binding properties are highly desirable to develop improved assays and enhance the predictive value of this diagnostic test.
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DC-SIGN binding properties were highly variable for milks derived from different mothers and between samplings from different geographical regions.
The binding properties were analyzed in competitive binding, internalization, and cell surface retention experiments.
The hypothesized binding properties were tested experimentally.
Thus, novel pocket descriptors allowing an in-depth characterization of binding sites are highly desired.
The binding assay conditions and radioligand binding assay are highly valuable to identify and design better HIV inhibitors for HAD.
These binding sites are highly charged.
These binding sites are highly conserved across the kinome.
Residues mediating Ub binding are highly conserved in OTULIN orthologs.
In contrast, MHC-binding peptides are highly stable.
The selected ligands have strong 99mTc and Re binding properties and the resulting complexes are highly stable in vivo both in terms of nuclease degradation and leaching of the metal.
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