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. 2018 Jan 17;10:456. doi: 10.3389/fnmol.2017.00456

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Copyright © 2018 Hagmeyer, Cristóvão, Mulvihill, Boeckers, Gomes and Grabrucker.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Hypothetical model for zinc-dependent anti-excitotoxic activity of S100B. In conditions of over-excitation, zinc is released from synapses in high amounts and calcium levels rise. Under these conditions, also S100B concentrations are found elevated. S100B may act as zinc buffering protein and upon zinc binding, the affinity for calcium binding is increased. Calcium binding of S100B may lower excitotoxic effects and thus promote neuronal survival. Excitotoxic calcium signaling was not altered in presence of S100B with mutated zinc binding sites and the effects on cell survival were abolished.