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Similarly, the PRC2 complex, which catalyzes H3K27me3, was shown to bind to pre-existing H3K27me3, and this binding appears to be crucial for the maintenance of this modification in proliferating cells [ 51, 52].
Thus, while both IP and pull-down experiments show that RAB26 binds ATG16L1 in a GTP-dependent manner, this binding appears to be weaker than the interaction between Rab33 and ATG16L1.
Importantly, we present evidence that these proteins participate in multiple, distinct PRC1 complexes, that several PRC1 complexes bind simultaneously to the INK4a locus, and that their binding appears to be interdependent.
Remarkably, CYC binds only to one of the two possible binding sites of the homodimeric complex and binding appears to be coordinated with the presence of ubiquinone at the Qi site.
However, for 11C-PBB3, non-displaceable (nonspecific) binding appears to be different between the gray and white matters [2].
Nevertheless, [11C]AF150 binding appears to be sensitive to changes in extracellular ACh levels, in particular when behavioural effects are apparent.
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The brain uptake of [11C]HMS011 was similar between monkeys and humans (peak SUV ~2), while the amount of specific binding appeared to be higher in monkeys than in humans [18].
Thus the distinct conformations of bH1 antibodies for dual binding appear to be at a similar energetic state.
Thus, neither the pattern of Vav1 redistribution, nor its tyrosine phosphorylation and SLP-76 binding, appear to be affected by the loss of intrinsic GEF activity (Fig. 3A E).
Results: FM550 bound human PPARγ, and binding appeared to be driven primarily by TPP.
For a given solubility characteristic, the degree of protein binding appeared to be the main determinant of circuit drug concentration.
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