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Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes

Dimeric ATP synthase accommodates itself to the membrane curvature in mitochondrial cristae along th

In a research article published in Proceedings of the National Academy of Sciences, USA, Tobias Spikes, Martin Montgomery and John Walker have shown how the mobility in the interfaces between monomers in dimeric bovine ATP synthase participates in forming the characteristic and ever-changing ultrastructure of inner mitochondrial membranes. This article has been selected by the PNAS as a research highlight.

Structural insights into the role of mitochondrial complex I in heart attack

A collaborative research project led by Professor Judy Hirst at the MBU, working with Mike Murphy (MBU) and Thomas Krieg (Medicine), provides important new insights into the cell damage that occurs during heart attacks. This work, published in Nature Communications with MBU PhD student Zhan Yin as first author, focuses on a version of mitochondrial complex I that contains a single amino acid mutation.

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