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. 2010 Mar 15;4:23. doi: 10.1186/1752-0509-4-23

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Copyright ©2010 Hendriks et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Alternate kinetic mechanisms. A, substrate inhibition (mechanism #1 in main text): MK2 and ATF2 are allowed to rebind p38 after phosphorylation. B, phospho-MK2 binds ATF2 (mechanism #2 in main text): phosphorylated MK2 is allowed to bind unphosphorylated ATF2 and prevent its interaction with p38. C, altered p38 (mechanisms #3-5 in main text): after phosphorylating MK2, p38 is left in an altered state such that it has either an altered affinity for ATP (mechanism #3 in main text; indicated by #), an altered affinity for ATF2 (mechanism #4 in main text; indicated by ##) or an altered catalytic rate for ATF2 (mechanism #5 in main text; indicated by ###).