Why F-ATP Synthase Remains a Strong Candidate as the Mitochondrial Permeability Transition Pore

Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal

(2018) Lishu Guo et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase

(2017) Jiuya He et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase

(2017) Jiuya He et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Atomic model for the dimeric FOregion of mitochondrial ATP synthase

(2017) Hui Guo et al.   SCIENCE

Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology

(2016) Alexander Hahn et al.   MOLECULAR CELL

Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy

(2016) Kutti R. Vinothkumar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

(2015) Matteo Allegretti et al.   NATURE

Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

(2015) Chimari Jiko et al.   eLife

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM

(2015) Anna Zhou et al.   eLife

F-ATPase ofDrosophila melanogasterForms 53-Picosiemen (53-pS) Channels Responsible for Mitochondrial Ca2+-induced Ca2+Release

(2014) Sophia von Stockum et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition

(2014) Michela Carraro et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mitochondrial Channels: Ion Fluxes and More

(2014) Ildiko Szabo et al.   PHYSIOLOGICAL REVIEWS

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore

(2014) K. N. Alavian et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Role of the c subunit of the FOATP synthase in mitochondrial permeability transition

(2013) Massimo Bonora et al.   CELL CYCLE

Dimers of mitochondrial ATP synthase form the permeability transition pore

(2013) V. Giorgio et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria

(2013) B. Daum et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae

(2012) K. M. Davies et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM

(2012) L. A. Baker et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria

(2012) D. M. Rees et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Dimer ribbons of ATP synthase shape the inner mitochondrial membrane

(2008) Mike Strauss et al.   EMBO JOURNAL