Sentence examples for binding to and sequestering from inspiring English sources

Third, since DNErbB4 works by binding to and sequestering the NRG ligand, NRG signaling will be reduced not only in DNErbB4 expressing cells, but also in the surrounding tissue.

For dynamic MTs, Colchicine prevents growth by binding to and sequestering free tubulin dimers.

These chimeric molecules act as decoys by binding to and sequestering RANKL, thus preventing it from interacting with its native receptor on hematopoietic osteoclast precursors and mature osteoclasts.

Moreover, by directly binding to and sequestering transcription factors, such as SMAD3, C/EBPα or vitamin D receptor, RUNX1-CBFA2T1 interferes with signal transduction pathways controlling differentiation and proliferation [ 8- 12].

At the mechanistic level, lncRNAs serve as "scaffolds" providing platforms to assemble RNA-protein complexes, "guides" to recruit RNAprotein complexes to target genes, and "decoys" by binding to and sequestering regulatory proteins away from their target DNA sequences [ 1, 2].

NRP-1 and NRP-2 are receptors for semaphorins, and can antagonise semaphorin action by binding to and sequestering VEGFs (Ellis, 2006; Guttmann-Raviv et al, 2006).

It has been shown that IGFBP-1a inhibits zebrafish embryo development by binding to IGFs and sequestering their binding to the IGF-I receptor [8].

Also, we observed a reduction in the rate of barbed end actin filament elongation in the presence 2 µM profilin-actin and soluble GFP-Lpd850−1250aa or GFP-LZ-Lpd850−1250aa, consistent with Lpd binding to (and partially sequestering) actin monomers.

The partial rescue of ibr5 defects observed when IBR5C129S was overexpressed might result from the IBR5C129S protein binding to and thus sequestering IBR5 substrate(s), as has been suggested for overexpression of the catalytically inactive MAPK phosphatase Pyp1C470S, which results in a phenotype similar to a loss-of-function allele of the substrate MAPK Spc1 in Schizosaccharomyces pombe [ 58, 59].

Mxd1 (Mand) and Mxi1 (Mare) are negative regulators of c-myc transcriptional activity and function by binding to Max and sequestering it from c-myc.

Usual mechanisms for handling toxic heavy metals include binding to metallothionein and sequestering in lysosomes.