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.
A Lethal Channel between the ATP Synthase Monomers / Nesci, Salvatore*. - In: TRENDS IN BIOCHEMICAL SCIENCES. - ISSN 0968-0004. - ELETTRONICO. - 43:5(2018), pp. 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.File in questo prodotto:
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