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Amidation can affect the turnover rate of secreted peptides and/ or affect the binding or activation of receptors by secreted peptides (reviewed by [77]).
Phosphorylation of both ER-α Ser118 and ER-α Ser167 occurs in response to either estradiol binding or activation of growth factor signaling pathways.
Likewise, while the suppression of G protein-mediated GPCR signaling may be related to binding or activation of β-arrestins by these dyes, it is unclear whether alternative interactions are also in play.
Taken together, the above results suggest that development of resistance to SINE compounds was not the result of mutations in the cargo binding pocket of XPO1 or other modification that reduced drug-target binding, or activation of a common multidrug resistance mechanism that exclude drug from the cell cytoplasm.
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None of the above work demonstrates specific binding to, or activation of, classical estrogen-signalling pathway factors in vivo.
Fourth, these aforementioned effects appear to be independent of binding to or activation of Tie2 and thus may work through a different and thus potentially novel mechanism.
Together, these data indicate that phosphorylation induced by either binding of EphB or activation of the FGFR can disrupt the association between ephrinB2 and TBC1d24.
By contrast, peptides consisting of repeating GPP motifs do not support platelet binding or activation, indicating an important contribution of the hydroxyl group to the affinity of CRP for GpVI.
Increased responsiveness in resistant cells may be due to a number of unexplored factors including expression of cell surface receptors capable of binding PSAP [ 51] or activation of specific signalling pathways [ 30].
Activation of SOC subsequent to ATP binding to a P2YR or activation of P2X7R [ 16] with BzATP (ATP was not studied as an agonist) is coupled to C6 chemokine production.
It has been reported that ER-α was significantly phosphorylated on Ser118 in response to either estradiol binding or the activation of the mitogen-activated protein kinase (MAPK) pathway, while Ser167 is phosphorylated by AKT, p90 ribosomal S6 kinase (RSK), and casein kinase II as well as MAPK [ 5, 7, 9, 24].
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