The mitochondrial permeability transition pore: channel formation by F-ATP synthase, integration in signal transduction, and role in pathophysiology
P Bernardi, A Rasola, M Forte… - Physiological …, 2015 - journals.physiology.org
The mitochondrial permeability transition (PT) is a permeability increase of the inner
mitochondrial membrane mediated by a channel, the permeability transition pore (PTP) …
mitochondrial membrane mediated by a channel, the permeability transition pore (PTP) …
The ATP synthase: the understood, the uncertain and the unknown
JE Walker - Biochemical Society Transactions, 2013 - portlandpress.com
The ATP synthases are multiprotein complexes found in the energy-transducing membranes
of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive …
of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive …
Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
J Zhao, S Benlekbir, JL Rubinstein - Nature, 2015 - nature.com
Abstract Eukaryotic vacuolar H+-ATPases (V-ATPases) are rotary enzymes that use energy
from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of …
from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of …
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation
G Cingolani, TM Duncan - Nature structural & molecular biology, 2011 - nature.com
ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy
metabolism in all kingdoms of life. Despite conservation of its basic structure and function …
metabolism in all kingdoms of life. Despite conservation of its basic structure and function …
Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures
S Arai, S Saijo, K Suzuki, K Mizutani, Y Kakinuma… - Nature, 2013 - nature.com
In various cellular membrane systems, vacuolar ATPases (V-ATPases) function as proton
pumps, which are involved in many processes such as bone resorption and cancer …
pumps, which are involved in many processes such as bone resorption and cancer …
Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation
J Symersky, V Pagadala, D Osowski, A Krah… - Nature structural & …, 2012 - nature.com
The proton pore of the F1Fo ATP synthase consists of a ring of c subunits, which rotates,
driven by downhill proton diffusion across the membrane. An essential carboxylate side …
driven by downhill proton diffusion across the membrane. An essential carboxylate side …
Structure of a thermophilic F1‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism
Y Shirakihara, A Shiratori, H Tanikawa… - The FEBS …, 2015 - Wiley Online Library
F1‐ATP ase (F1) is the catalytic sector in FoF1‐ATP synthase that is responsible for ATP
production in living cells. In catalysis, its three catalytic β‐subunits undergo nucleotide …
production in living cells. In catalysis, its three catalytic β‐subunits undergo nucleotide …
Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1–ATPase from bovine heart mitochondria
DM Rees, MG Montgomery… - Proceedings of the …, 2012 - National Acad Sciences
The molecular description of the mechanism of F1–ATPase is based mainly on high-
resolution structures of the enzyme from mitochondria, coupled with direct observations of …
resolution structures of the enzyme from mitochondria, coupled with direct observations of …
ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides
Z Ahmad, F Okafor, S Azim… - Current medicinal …, 2013 - ingentaconnect.com
In this review we discuss the role of ATP synthase as a molecular drug target for natural and
synthetic antimicrobial/antitumor peptides. We start with an introduction of the universal …
synthetic antimicrobial/antitumor peptides. We start with an introduction of the universal …