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When bulky inhibitors are needed to bind a large protein pocket, such inhibitors are structurally complex and generally commercially unavailable.
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APC is a large protein that binds to both β-catenin and AXIN1.
It is a large protein including 11 zinc fingers which it uses to bind to the DNA.
MHC binds small peptides that are typically cleaved from a larger protein [ 20].
Since the p62 protein can bind a large number of proteins through its multiple protein protein interaction motifs (Moscat et al. 2006), including both LC3 and ubiquitin (Komatsu et al. 2007a), the ubiquitin- and LC3-binding protein "p62" regulates the formation of protein aggregates and is removed by autophagy (Komatsu et al. 2007a).
It is now well established that proteins are removed from the tubular fluid by receptor-mediator endocytosis via megalin, a receptor known to bind a large variety of proteins, including albumin, metallothionein and the LMW proteins used for screening tubular proteinuria [ 24, 25].
Further, it is known to bind a large number of proteins with high specificity implying that its intrinsic mechanism of binding is finely tuned to respond to its diverse set of targets.
On the other hand, studies have shown that nanowires readily bind the large protein fibronectin and are readily internalized when incubated with mammalian cells [ 10].
Furthermore, in the LRPs, these repeats bind to large protein complexes like the α2 macroglobulin-protease complexes and urokinase-type plasminogen activator-plasminogen activator inhibitor (uPA-PAI) [ 53, 54].
Once crRNAs are generated, they bind a large multisubunit complex of Cas proteins called Cascade and target it to matching DNA of viruses and plasmids, ultimately leading to its destruction [ 13].
Each MHC protein can bind a large set of different peptides.
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