Mitochondrial F-type ATP synthase: multiple enzyme functions revealed by the membrane-embedded FO structure
Author:
Affiliation:
1. Department of Veterinary Medical Sciences, University of Bologna, Bologna, Italy
Funder
CARISBO Foundation
Publisher
Informa UK Limited
Subject
Molecular Biology,Biochemistry
Link
https://www.tandfonline.com/doi/pdf/10.1080/10409238.2020.1784084
Reference86 articles.
1. An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore
2. Mitochondrial Ca2+‐activated F1FO‐ATPase hydrolyzes ATP and promotes the permeability transition pore
3. Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase
4. Mitochondrial ATP synthase dimers spontaneously associate due to a long-range membrane-induced force
5. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits
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