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Locals also believe that the bile's toxicity can be activated by interactions with other substances.
Reporter strain KS1 [12] carries a chromosomal lacZ gene under the control of a promoter that can be activated by interactions between a protein fused to λ cI and a protein fused to the α subunit of RNA polymerase.
These differences in soluble receptor release may have important consequences for TNF-α signalling (e.g. increased release of sTNF-RII may reduce the ability of cells to be activated by interactions with membrane bound TNF-α on surrounding cells) [ 42].
This hypothesis is supported by numerous studies showing that PI3K1A may indeed be activated by interactions of p85-SH3 domains with proline-rich domains of several other proteins, and by previous data suggesting that a specific proline-rich domain of the α-subunit of Na+/K+-ATPase (TPPPTTP) may be involved in dopamine-induced internalization of Na+/K+-ATPase at the clathrin-coated pits.
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It has been reported that latent TGF-β can be activated by interaction with αvβ3 and αvβ5 integrins that are overexpressed in cultured SSc dermal fibroblasts [ 28, 29].
The expression of these proteases is tightly regulated and can, for example, be activated by interaction of the glioma cell with the surrounding ECM.
The maize MIK gene codes for a GCK-like MAP4K that can be activated by interaction with maize atypical receptor kinase (MARK) [ 49].
c-Abl can be activated by interaction with its substrates [ 16], and we observed that wild-type c-Abl, as well as dominant-active c-Abl (lacking the SH3 domain) and kinase-inactive c-Abl, coprecipitated with GST-Lpd.
TGF-β is produced initially as a pro-protein which is cleaved by furin-like proteases to yield a small latent complex consisting of dimeric TGF-β which is concealed by two latency associated peptides (LAP), This inactive complex can be activated by interaction with the αvβ6 integrin 39– 41 which can bind an RGD motif on the LAP leading to a conformational change.
An alternative possibility is that immune cells were activated by interactions between intact hemagglutinin of vaccines with sialic acid or other receptors on immune cells via an activation pathway independent of TLR7.
In this mechanism a zinc-bound water molecule is activated by interactions with Asp-320 and His-269, whereas the formimino group of the substrate is activated by interaction with Glu-235.
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