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Protein scaffold interactions that enhance BMP binding are of the utmost importance, since prolonged BMP release creates the most osteogenic microenvironment.
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Semi-quantitative analysis indicate that binding was of the same rank of order between Cntn5 and Cntn6 (Fig. 7B).
Temperature, pH, and ligand binding are some of the environmental cues that have been used to trigger changes in hydrogels.
The result of such binding is the modification of the activity of the partner, the assembly of a complex or local posttranslational modification of the IDP [14], [15].
However, the difference of the binding was remarkable of the three groups.
The locations of significant binding were independent of the input function used.
Research on drug-protein binding is one of the important contents in the study of early stage clinical pharmacokinetics of drugs.
Protein binding is one of the key elements that affects biodistribution of the nanoparticles throughout the body.
F-actin binding is one of the common properties of coronin proteins.
Such binding is one of the mechanisms used by the host immune system to fight aberrant proliferating tumour cells.
Protein binding is one of the key elements affecting biodistribution, biocompatibility, and therapeutic efficacy of the NMs [ 72, 73].
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