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BREC also express P lGF-1 which can be stimulated by binding of VEGF to VEGF receptor (VEGFR) 2 [ 19, 20].
Most of these activities are known to be stimulated by binding to a number of different integrins via the RGD sequence (αv β3, αv β1, αv β5) or via RGD-independent interactions (α4 β1, α9 β1, and α8 β1).
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The kinase activity of PAK is stimulated by binding to activated Rac1.
The polymerization of CtpS is stimulated by binding its product, CTP, and disrupted by binding its substrates, UTP and ATP.
Mec1 and its homologue ATR are stimulated by binding to Dpb11 and TopBP1, respectively (Kumagai et al, 2006; Mordes et al, 2008; Navadgi-Patil and Burgers, 2008).
The ATPase activity of the clamp loader is stimulated by binding both to the clamp and to DNA [ 39, 40], and upon ATP hydrolysis the affinity of the clamp loader for both clamp and DNA is greatly diminished, leading to ejection of the clamp from the clamp loader.
Sumoylation of PARP-1 is stimulated by binding to intact, but not to damaged DNA.
These kinases include the evolutionarily conserved p21-activated serine/threonine kinase (PAK), which is stimulated by binding to Cdc42 and Rac, and the Rho-binding serine/threonine kinase.
While in animal cells F-actin polymerization is stimulated by binding of capping protein to PIP2, plant actin capping protein is inhibited by PA.
The destruction complex is disrupted when active Wnt signaling is stimulated by binding of Wnt proteins to its Frizzled receptor on the cell membrane.
For example, brevican exposed its promigratory attributes after cleavage by members of the ADAMTS protease family [ 44] and glioma migration on laminin is stimulated by binding of glycosaminoglycans [ 45].
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