A Lethal Channel between the ATP Synthase Monomers
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Updated: Feb 13, 2026

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
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1Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra 50, 40064 Ozzano Emilia (BO), Italy.
Trends in Biochemical Sciences
|March 21, 2018
Abstract:
The molecular structure of the transmembrane domain of ATP synthases is responsible for the inner mitochondrial membrane bending. According to the hypothesized mechanism, ATP synthase dissociation from dimers to monomers, triggered by Ca2+ binding to F1, allows the mitochondrial permeability transition pore formation at the interface between the detached monomers.
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