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SENP5 negatively modulates Drp1 SUMOylation and mitochondrial fission Although SUMOylation is predominantly a nuclear protein modification and most SUMO-regulated cellular processes occur in the nucleus, there is increasing recognition that the SUMOylation machinery and substrates are present and active in extranuclear compartments

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Acknowledgments The authors are grateful to the Core Facility Center, Office of the Research and Development, Taipei Medical University, for its great support in TOF-SIMS analysis

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