Sentence examples for binding to the apc from inspiring English sources

Mps1 degradation is in part mediated by the APC activator Cdh1, whose binding to the APC requires dephosphorylation by Cdc14.

This idea is supported by the finding that Mad2 prevents Cdc20 binding to the APC in an in vitro assay using purified budding yeast components (Foster and Morgan 2012).

Seven out of a cluster of nine amino acid residues in the Gla domain of PS that have been identified as being of critical importance for putative binding to the APC Gla domain are identical in the GAS6 Gla domain (Leu21/Arg28/Asn33/Asp34/Pro35/Tyr41/Leu45), whereas the other two residues are highly conserved (Asn23/Lys24 in PS; Ser23/Arg24 in GAS6) [ 2, 3].

The consequence of calcium binding to the regulatory domain of APC is a stimulation of the substrate transport activity of the carrier [2,4,7].

The phenomena mentioned above consist of (1) the expression of the CTLA-4 receptor on the surface of a T-cell, which after binding to the protein B7 on APCs transducts the inhibitory signal to the nucleus and (2) the expression of the PD-1 receptor on the T-cell surface which may lead to the inactivation of the T-cell after binding to the PD-L1 (programmed cell death 1 ligand) on tumor tissue.

The CHO cells were then stably transected by PDR2EF1α ESAT-6:Fcγ1 vector using lipofectamin and the expression and its binding to the Fcγ receptor (FcγRI) on APCs were confirmed by immunofluorescence assay (IFA).

Following the localization of BUB1, MAD1 then lowers the energy barrier of MAD2 and triggers MAD2 conformational change, allowing MAD2 binding to the APC/C activator CDC20.

In normal mitosis Cdh1 is prevented from binding to the APC/C through direct inhibitory phosphorylation by Cyclin B1-Cdk1 [25], [26], but mitotic exit and activation of APC/C-Cdh1 can be initiated by the addition of a Cdk-inhibitor to prometaphase cells [42].

Because we showed earlier that APC3 is essential for cyclin B1 binding to the APC/C, we conclude from these data that cyclin B1 in particular requires hyper-phosphorylation of APC3 to bind the mitotic APC/C.

This adds to the accumulating evidence that substrate binding to the APC/C requires the cooperation of multiple interaction motifs (Burton and Solomon, 2001; Hames et al., 2001; Sedgwick et al., 2013; Wolthuis et al., 2008).

Thus, in addition to binding to the APC/C, cyclin A also recruits Cdc20 (Di Fiore and Pines, 2010; Wolthuis et al., 2008), and Nek2A can be degraded in trans when the amino-terminus of Cdc20 or the related protein, Cdh1 are added to activate the APC/C (Kimata et al., 2008).