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.

Nesci, S. (2018). A Lethal Channel between the ATP Synthase Monomers. TRENDS IN BIOCHEMICAL SCIENCES, 43(5), 311-313 [10.1016/j.tibs.2018.02.013].

A Lethal Channel between the ATP Synthase Monomers

Nesci, Salvatore
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.
2018
Nesci, S. (2018). A Lethal Channel between the ATP Synthase Monomers. TRENDS IN BIOCHEMICAL SCIENCES, 43(5), 311-313 [10.1016/j.tibs.2018.02.013].
Nesci, Salvatore*
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/632141
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