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Camelids and sharks possess a class of unconventional immunoglobulins consisting of heavy-chain homodimers in which antigen binding is mediated through a single variable domain.
Three candidate ribosome receptors, p180, p34, and Sec61p, have been identified in binding studies with inactive ribosomes, suggesting that ribosome binding is mediated through a receptor-ligand interaction.
This binding is mediated through zinc finger motifs [ 8, 9].
In each of these domains, phosphoinositide binding is mediated through pockets that are strategically lined with basic residues formed by two distal β loops.
This molecule also acts as a receptor for the pathogen and binding is mediated through the bacterial OMP member, SabA [ 26].
Gamete recognition and binding is mediated through GPI-anchored P47 on female interacting with P230, complexed to GPI-anchored P48/45 on the male cell.
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Furthermore, excessive CC49 antibody successfully blocked the binding of CC49-QDs to the MGC80-3 cells, indicating that the binding was mediated through TAG-72.
The effects of VEGF receptors after ligand binding are mediated through receptor tyrosine autophosphorylation.
EGFR binding (F10) is mediated through the binding of a mitogenic peptide epidermal growth factor (EGF) to a surface membrane receptor, EGFR of breast cancer cells [ 49].
As GATA-2 DNA binding activity is mediated through the C-terminal zinc finger domain [ 1], the mutated GATA-2 is predicted to be defective in DNA binding.
Because ANXA1 also has HAUSP-binding motif sequences (AMVS and ALLS) on its N-terminal region and annexin conserved domain, we assumed that the binding of ANXA1 to HAUSP is mediated through HAUSP-binding motifs.
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