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The binding of these integrins to a particular ECM protein during cell adhesion can be complex phenomena, but usually involves the recognition of a specific target sequence of the ligand (ECM components; Singleton and Menino 2005).
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The binding of integrin and integrin liposomes to these surfaces resulted in a decrease in the resonance frequency and a dissipation increase, which were, however, less pronounced than for the Fg coatings.
Furthermore, we show that it does so by binding to, and blocking ECM binding of, the integrin αv β3 on ECs.
Talin is an adaptor protein recruited to adhesions after the binding of β1 integrins to collagen (Craig and Johnson, 1996) and other matrix ligands.
Through a complex series of interactions involving binding of selectins, integrins, and adhesion molecules, the neutrophil rolls, arrests, and migrates through the endothelial barrier [ 3- 6].
Whether binding of integrins to VDCCs and TRPCs influences permeability of these channels remains however unknown.
Binding of cell-surface integrins is necessary for FN fibrillogenesis; e.g., antibodies that prevent binding of FN to integrins inhibit the formation of FN fibrils in vitro [8].
Since R50E can still bind to FGFR1 and heparin [12], it is likely that the defect in integrin binding is related to its antagonistic action in FGF signaling, and that crosstalk between integrins and FGFR is mediated by the direct binding of integrins to FGF.
Studies on migrating CHO cells transfected with β1 and β3 integrins suggest that the Ca2+-activated calpain could be involved in the dissociation between integrins and cytoskeleton, and thereby could influence the binding of integrins to their ligands.
These findings suggest that the direct binding of integrins to WT FGF1 plays a role in sustained activation of the entire FGF signaling pathway.
There is increasing evidence that some of these effects are mediated through signals elicited by the binding of integrins to their target proteins.
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