Sentence examples for binding to surface nucleolin from inspiring English sources

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Finally, ligand binding to surface nucleolin could generate high transitory intracellular Ca2+ membrane fluxes involving SOC-like channels, and thus initiate signaling events [15].

Following binding to surface nucleolin, HB-19 is internalized and is concentrated in the cytoplasm without translocation into the nucleus (Figures 2C, 3C).

After specifically binding to surface nucleolin, HB-19 enters cells and accumulates in the cytoplasm but it does not cross the nuclear membrane.

The difference between subcellular localization of HB-19 and endostatin could be accounted by the nature of interaction with surface nucleolin, since endostatin but not HB-19 binding to surface nucleolin requires heparan sulfate proteoglycans [21], [28].

Besides its well-documented role in the internalization of specific ligands, we recently reported that ligand binding to surface nucleolin could also induce calcium entry into cells, a process inhibited by chelating calcium from the culture medium [15].

Indeed, after specifically binding to surface nucleolin, HB-19 and related Nucant pseudopeptides enter cells and accumulate in the cytoplasm without crossing the nuclear membrane.

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These results indicate that Nucant binds nucleophosmin independently of its capacity to bind to surface nucleolin.

Moreover, the binding affinity of Nucant to nucleophosmin is much lower compared to its binding affinity to surface nucleolin.

As Nucleolin is shown to bind Ca2+ [59], [59], and is involved in epidermal Ca2+ homeostasis [60], it remains to be shown whether binding of calcium to surface nucleolin is a necessary step for ligand internalization via surface nucleolin.

Consequently, the binding of HB-19 to surface nucleolin could also affect the organization of nucleolin-associated proteins in this 500-kDa complex and thus generate more inhibitory mechanisms.

This and the capacity of HB-19 to bind surface nucleolin without dissociating the 500-kDa complex suggest that the binding of HB-19 to surface nucleolin could change the organization of the 500-kDa complex, and thus interfere with the proper functioning of nucleolin and the nucleolin associated proteins.

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