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Each gene G i can bind up to two copies of its repressing protein, with cooperative binding.
We take the assumption that each domain i can bind an effector protein E 1 i which in turn can recruit another effector protein E 2 i till finally E m − 1 i binds E m i.
In vitro, TRAPP I can bind COPII vesicles by binding the coat Sec23p subunit [ 95] and this could be the first event before interaction of the vesicle with its target [ 76].
The inhibitor (I) can bind to either E or ES with the dissociation constants Ki or Ki', respectively.
While sCD23 has to trimerize to develop considerable affinity for its ligand [1], sFcεRI can bind IgE with a one-to-one ligand-receptor ratio.
Another proposed role is in relation to chromosomal structure, because both DNA gyrase and DNA polymerase I can bind to REP elements [ 64, 65].
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RIG-I can bind to select RNAs in a native gel electrophoresis [7].
Importantly, RIG-I can bind these RNAs without activating signaling, due to the proofreading mechanism imparted by ATP hydrolysis.
On the one hand, excess of cholesterol and cholesterol crystals can activate Toll-like receptors (TLR) and APOE and APOA-I can bind and neutralize TLR ligands and inhibit the induction of inflammatory cytokines (Azzam & Fessler, 2012).
The COL-I was noted to be able to bind with the cell surface integrin and activate a series of intracellular signal pathways, for example, COL-I can bind with α2 β1 via its GFOGER motif to direct cellular behavior [ 23].
However, it was not identified whether (i) eEF1α can bind RNA independently, (ii) whether eEF1α requires other proteins to successfully generate a binding complex, or (iii) if specific single or multiple domain(s) of eEF1α are responsible for RNA interactions.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com