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The AC family of proteins binds both globular (G-Actin) and filamentous actin (F-actin) and this binding is regulated by multiple mechanisms: phosphorylation, interaction with polyphosphoinositides, pH, and competitive binding interactions with other actin binding proteins [13], [14].
Furthermore, the binding kinetics of 15 mutants revealed that binding is regulated by long-range interactions, which can be correlated with the structural rearrangements resulting from peptide binding.
Vector release or binding is regulated by the effective affinity of the vector for the polymer, which depends upon the strength of molecular interactions.
King, J.M., T.S. Hays and R.B. Nicklas, Dynein is a transient kinetochore component whose binding is regulated by microtubule attachment, not tension, Journal of Cell Biology, vol. 151 (2000), pp. 739-748.
Transcription factor binding is regulated by several interactions, primarily involving cis-element binding.
The specificity of aldosterone-MR binding is regulated by cortisol levels and 11 β-HSD2 enzyme expression.
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Expression of PDR16 and its mutant allele, defective in PI binding were regulated by native PDR16 promoter.
The nucleotide binding state is regulated by PPIs with guanine nucleotide exchange factors (GEF), which mediate a GDP to GTP exchange, or by GTPase-activating proteins (GAP), which promote hydrolysis of bound GTP to GDP.
The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.
This is possibly due to the fact that the activity of the GTP-binding protein Era is regulated by binding of GTP [ 24].
Yet, MDC1 binding to γH2A.X is regulated by another phosphorylation event at Y142, preventing MDC1 from binding to the phosphorylated S139 [101].
More suggestions(16)
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binding is displaced by
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binding is limited by
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