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A disassociated NK cell can restart and bind to new targets and finally eliminate them, commonly referred to as recycling capacity or killing frequency [2].
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It has been found that high levels of Myc bind to a new set of target genes, suggesting that the behavior of Myc depends on its level [132, 133].
Protein interaction domains excel in the former role because they bind their cognate ligands with high affinity and specificity, and some can be engineered to recognize new targets.
Literature-mining studies show that a large majority of new drugs bind to targets in some way related to a previously existing one [ 5- 7].
Specifically, we argue that major extraretinal inputs to the LGN may provide: (1) eye movement information to enhance and bind visual signals related to new saccade targets and (2) top-down and bottom-up information about target relevance to selectively enhance visual signals through spatial attention.
Solid-phase radiolabeling binding assays to test IG3 ability to bind to its targets.
(E) Statistical analyses of the target number of ligands included in the MTLD: 795 ligand entries bind two targets; 551 ligand entries bind 3 5 targets; 189 ligand entries bind 6 10 targets; and 197 ligand entries bind to >10 targets; (F) Comparison of the conformation of a ligand bound to different targets.
This (indirect) diversity measure has its disadvantages as similar ligands can bind to different targets or alternatively, structurally diverse ligands may bind to the same target.
According to the similar property principle, similar ligands are expected to bind to similar targets [3].
CaM and CaM-like proteins bind to their targets by anchoring hydrophobic residue of the target.
Drugs that bind to common targets likely exert similar activities.
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