Sentence examples for binding is proposed to from inspiring English sources

In mammalian cells regulation of AP-2 cargo binding is proposed to occur by phosphorylation of the Thr156 residue which lies in the hinge region between the N-terminal longin and C-terminal mu adaptin homology domain.

The ability of these systems to bind DNA with different binding modes is proposed to affect their function in vivo.

Within the C-terminus of the channel, a partially overlapping binding domain for calmodulin allows Ca2+-calmodulin binding and is proposed to destabilize the open state.

The present minor-groove binding mode is proposed to represent the initial surface interactions of binuclear RuII compounds prior to intercalation into AT-rich DNA.

It has a functional ATPase domain and its nucleotide binding site is proposed to regulate activity of the R-protein in pathogen recognition.

The molecular basis for this alteration in RNA-binding properties is proposed to result from the inability of the RNA to induce a change in the structure of the free protein to produce a high-affinity complex.

The phosphate-binding site is proposed to be located near the active site cleft, between strands β1 and β2 (Fig. 1A; [1A]).

pGSN together with Gc-globulin, another extracellular actin-binding protein, is proposed to function as an 'extracellular actin scavenger system' responsible for the removal of actin released during tissue injury [ 15].

The increased tumor binding of 111In-DOTA-DAB4 111In-DOTA-DAB4 111In-DOTA-DAB4om a sisnificant increase in the number and strength of DAB4 binding targets, which was related to both the proposedmotoerapy number of dead tumor cells as well as thavextent to which the La autoantigen was induced in each dying cell.

Based on the X-ray crystal structure of the adducts of hCA II with ureate and hydroxamate inhibitors, the hypothetical binding of hydroxyurea is proposed to be achieved in deprotonated state, with the nitrogen atom coordinated to Zn II), and the OH group of the inhibitor making a hydrogen bond with Thr 199.

Nucleotide binding to Hsp90 is proposed to alter its conformation and define the subset of chaperones with which it interacts (16).