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- W2011015136 abstract "Significance The question as to how the proton motive force in mitochondria is distributed among the proteins that require a proton gradient for their work is one of the central unresolved questions in mitochondrial physiology and important for the mechanistic insight in the function of mitochondrial proteins. Our results suggest that the local separation of the proteins on the inner mitochondrial membrane makes it impossible for uncoupling protein 4 (UCP4) to uncouple phosphorylation from proton pumping. Nonetheless, UCP4 should be well able to shortcut excessive transmembrane proton gradients to thereby regulate reactive oxygen species production. It explains how the proton transporter may fulfill that function without being a real UCP like UCP1." @default.
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- W2011015136 date "2014-12-22" @default.
- W2011015136 modified "2023-10-11" @default.
- W2011015136 title "Superresolution microscopy reveals spatial separation of UCP4 and F <sub>0</sub> F <sub>1</sub> -ATP synthase in neuronal mitochondria" @default.
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- W2011015136 doi "https://doi.org/10.1073/pnas.1415261112" @default.
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