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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).
Two molecular functions, structural molecular activity and carbohydrate binding, appear to be elevated significantly in the infected library (Table 6).
Interestingly, the different effects of the tetra- and dihydropteridines on tight pterin binding appear to be mirrored by the effects on the formation of SDS-resistant dimers, which also required the tetrahydro- derivatives.
Similarly, the lack of APP and TrkA phosphorylation and the consequent reduction in their binding appear to be related to an age-dependent decrease in the expression levels of TrkA in Y682G mice and to the degeneration of cholinergic fibers with an associated decline in cognitive and neuromuscular performance 9.
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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.
Nevertheless, [11C]AF150 binding appears to be sensitive to changes in extracellular ACh levels, in particular when behavioural effects are apparent.
However, for 11C-PBB3, non-displaceable (nonspecific) binding appears to be different between the gray and white matters [2].
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