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The potency of a T cell is determined in large part by two interactions, binding of a cognate peptide to the MHC, and binding of the T cell receptor (TCR) to this pepMHC.
The activity of each CDK depends on the binding of a cognate cyclin[1], [2].
G protein coupled receptors (GPCRs) are heptahelical cell surface receptors that, upon extracellular binding of a cognate ligand, initiate intracellular signal transduction pathways via heterotrimeric G proteins.
Substrate phosphorylation has previously been reported to recruit the SUMO E2 enzyme Ubc9, through the binding of a cognate basic patch on Ubc9.
In the first elongation cycle, EF-Tu accelerates the binding of a cognate aminoacyl(aa -tRNA, in the form of aa -tRNANA·EF-Tu·GTP ternary complex (TC), to the rinosomal A/theite oform70S initiatiof complex (70SIC), which contanns initiaa-tRNA·EF-Tu·GTPternary in the ribosomal P-site.
Binding of a cognate substrate leads to the displacement of the inhibitory chloride anion, possibly by using the carboxyl moiety of derivingving from the consensus cleavage site (Q[F,I,L,V]D|G1'X2'X3'D4').
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In this model, any serendipitous binding of a non-cognate, self RNA (for example, a stem-loop structure) directly to RIG-I hel (Fig. 6b, step 2b) would be rapidly counteracted by RNA dissociation from RIG-I by the ATPase motor (Fig. 6b, step 3b) in an irreversible manner, because non-cognate, self RNA would lack the strong triphosphate anchoring to the CTD.
To directly prove binding of Gfi1 to a cognate binding site in the IL7Rα gene, we performed chromatin-immunoprecipitation studies in progenitor B cell extracts from Gfi1+/+ mice.
EphrinB1 can be tyrosine phosphorylated in response to binding the extracellular domain of a cognate Eph receptor44,45, the tight-junction-associated protein Claudin46 or in response to FGFR activation47.
Most often, PI3K is activated via the binding of a ligand to its cognate receptor, whereby p85 associates with phosphorylated tyrosine residues on the receptor via a Src- homology 2 (SH2) domain.
We next showed that CGRRAGGSC-phage binding to IL-11Rα is mediated by the IL-11-like motif, because synthetic CGRRAGGSC inhibited binding of the cognate phage in a concentration-dependent manner (Figure 1B).
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