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A remaining open question is to extend the present analysis to the case where many binding molecules can trap receptors.
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Filamins are an actin cross-linker, and serve as scaffolds for many binding partners including channels, receptors, intracellular signaling molecules, and transcription factors [ 13, 14].
Many PDZ proteins can also influence the phosphorylation of their binding molecules.
Though many binding sites exhibit specificity required for their biological function, other molecules require less specificity to fulfill their purpose.
DARPins comprise a novel class of binding molecules suitable to complement or even replace antibodies in many biotechnological or biomedical applications.
Carlson, C. D. et al. Specificity landscapes of DNA binding molecules elucidate biological function.
Many small molecules bind in the T4 binding pocket of TTR and prevent its aggregation and amyloidogenesis cascade by stabilizing the native tetramer [ 27– 29].
At high concentrations an opposite effect may arise in which steric hindrance from many molecules binding reduces their passage through the sheet interstices.
Another mechanism of regulation of initiation involves the binding of many DnaA molecules to a chromosomal locus, datA, thereby reducing the number of DnaA molecules accessible to oriC [30], [31].
Many signaling molecules regulate their binding to protein partners through tyrosine phosphorylation.
Identifying kinase inhibitors that target the ATP-binding site of a kinase can be fraught with specificity problems because all kinases and many other molecules possess ATP-binding sites.
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