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. 2010 Aug 6;5(8):e11905. doi: 10.1371/journal.pone.0011905

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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A: Self association studied by analytical ultracentrifugation. Shown are sedimentation velocity data. The sedimentation coefficients have been normalized to standard condition. Peaks corresponding to the MST4 monomer and dimer are indicated by “M and D” respectively. B: Autophosphorylation of MST4 studied by ESI-MS. The mass of the unmodified protein (33.818 Da) has been indicated. In addition to the three detected phosphorylation events the protein also oxidized (+16 mass shifts indicated by *).