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However, in DLD-1 cells expressing FAK and PYK2, simultaneous KD of both kinases were required to inhibit GSK3Y279/Y216 phosphorylation and to reduce the level of β-catenin, strongly suggesting that FAK and PYK2 function redundantly to phosphorylate GSK3Y279/Y216 to promote Wnt/β-catenin signaling.
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Thus, both kinases are required in the process.
Furthermore, both kinases are required to inactivate GSK3β completely, and so turn on the Wnt signaling pathway.
Finally, one could also envisage that both kinases are required at different locations around the DSB, to establish a proper γH2AX domain.
Given that both kinases are required for bi-orientation, they may target different substrates at kinetochores (or Mps1 may do so at spindle poles; Supplemental Results and Discussion, note 12) or different sites of the same substrates, to promote re-orientation of kinetochore-spindle pole connections.
To determine which kinases were required for Id1 mediated HMVEC chemotaxis, cells were incubated with chemical signaling inhibitors.
Thus, all these kinases were required broadly for ESC differentiation towards mesoderm and endoderm, but only PI3K appeared specific to the transition between mesendoderm and committed ADE.
We therefore asked whether the activity of both these kinases is required in the presence and absence of functional pRb.
Activation of both of these kinases is required for NF-κB and MAPK activation.
These results suggest that T451 phosphorylation by ABA-activated kinases is required for stability of ABF3.
Plk4 itself but possibly other kinases are required for phosphorylation of this important motif [33].
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