Related references
Note: Only part of the references are listed.Protein folding and unfolding: proline cis-trans isomerization at the c subunits of F1FO-ATPase might open a high conductance ion channel
Salvatore Nesci
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2022)
Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases
J. Kishikawa et al.
NATURE COMMUNICATIONS (2022)
What happens when the mitochondrial Hthorn-translocating F1FO-ATP(hydrol)ase becomes a molecular target of calcium? The pore opens
Salvatore Nesci
BIOCHIMIE (2022)
F1FO ATP synthase molecular motor mechanisms
Wayne D. Frasch et al.
FRONTIERS IN MICROBIOLOGY (2022)
What happens when the mitochondrial H+-translocating F1FO-ATP(hydrol)ase becomes a molecular target of calcium? The pore opens
Salvatore Nesci
BIOCHIMIE (2022)
1,5-Disubstituted-1,2,3-triazoles as inhibitors of the mitochondrial Ca2+-activated F1FO-ATP(hydrol)ase and the permeability transition pore
Vincenzo Algieri et al.
ANNALS OF THE NEW YORK ACADEMY OF SCIENCES (2021)
C subunit of the ATP synthase is an amyloidogenic calcium dependent channel-forming peptide with possible implications in mitochondrial permeability transition
Giuseppe Federico Amodeo et al.
SCIENTIFIC REPORTS (2021)
The mitochondrial permeability transition pore in cell death: A promising drug binding bioarchitecture
Salvatore Nesci
MEDICINAL RESEARCH REVIEWS (2020)
Molecular dynamics simulation of proton-transfer coupled rotations in ATP synthase FO motor
Shintaroh Kubo et al.
SCIENTIFIC REPORTS (2020)
ATP synthase c-subunit ring as the channel of mitochondrial permeability transition: Regulator of metabolism in development and degeneration
Nelli Mnatsakanyan et al.
JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY (2020)
Cryo-EM structure of the entire mammalian F-type ATP synthase
Gergely Pinke et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2020)
Chromophore-Assisted Light Inactivation of the V-ATPase V0c Subunit Inhibits Neurotransmitter Release Downstream of Synaptic Vesicle Acidification
Sylvain Rama et al.
MOLECULAR NEUROBIOLOGY (2019)
The macrophage-specific V-ATPase subunit ATP6V0D2 restricts inflammasome activation and bacterial infection by facilitating autophagosome-lysosome fusion
Yu Xia et al.
AUTOPHAGY (2019)
Structure and Mechanisms of F-Type ATP Synthases
Werner Kuehlbrandt
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 88 (2019)
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling
Bonnie J. Murphy et al.
SCIENCE (2019)
Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion
Gregory E. Miner et al.
TRAFFIC (2019)
ATP Synthase C-Subunit-Deficient Mitochondria Have a Small Cyclosporine A-Sensitive Channel, but Lack the Permeability Transition Pore
Maria A. Neginskaya et al.
CELL REPORTS (2019)
Cryo-EM studies of the rotary H+-ATPase/synthase from Thermus thermophilus
Atsuko Nakanishi et al.
BIOPHYSICS AND PHYSICOBIOLOGY (2019)
Calcium and regulation of the mitochondrial permeability transition
Valentina Giorgio et al.
CELL CALCIUM (2018)
Protonation-dependent stepped rotation of the F-type ATP synthase c-ring observed by single-molecule measurements
Seiga Yanagisawa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
From ATP synthase dimers to C-ring conformational changes: unified model of the mitochondrial permeability transition pore
Giuseppe Federico Amodeo et al.
CELL DEATH & DISEASE (2017)
The Presynaptic v-ATPase Reversibly Disassembles and Thereby Modulates Exocytosis but Is Not Part of the Fusion Machinery
Anna Bodzeta et al.
CELL REPORTS (2017)
Oscillating Electric Field Measures the Rotation Rate in a Native Rotary Enzyme
Csilla-Maria Ferencz et al.
SCIENTIFIC REPORTS (2017)
Mitochondrial permeability transition involves dissociation of F1FO ATP synthase dimers and C-ring conformation
Massimo Bonora et al.
EMBO REPORTS (2017)
Ca2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition
Valentina Giorgio et al.
EMBO REPORTS (2017)
Relating proton pumps with gap junctions: colocalization of ductin, the channel-forming subunit c of V-ATPase, with subunit a and with innexins 2 and 3 during Drosophila oogenesis
Julia Lautemann et al.
BMC DEVELOPMENTAL BIOLOGY (2016)
Calcium and reactive oxygen species in regulation of the mitochondrial permeability transition and of programmed cell death in yeast
Michela Carraro et al.
CELL CALCIUM (2016)
F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements
Mitsuhiro Sugawa et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore
Sergio Couoh-Cardel et al.
SCIENTIFIC REPORTS (2016)
Operating principles of rotary molecular motors: differences between F-1 and V-1 motors
Ichiro Yamato et al.
BIOPHYSICS AND PHYSICOBIOLOGY (2016)
ATP Synthase
Wolfgang Junge et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 84 (2015)
Structure of the Vacuolar H+-ATPase Rotary Motor Reveals New Mechanistic Insights
Shaun Rawson et al.
STRUCTURE (2015)
Autophagosome-lysosome fusion is independent of V-ATPase-mediated acidification
Caroline Mauvezin et al.
NATURE COMMUNICATIONS (2015)
Optimization of neuronal cultures from rat superior cervical ganglia for dual patch recording
Julien Amendola et al.
SCIENTIFIC REPORTS (2015)
A functional screen for copper homeostasis genes identifies a pharmacologically tractable cellular system
Ulrich Schlecht et al.
BMC GENOMICS (2014)
Transcriptional regulation of the V-ATPase subunit c and V-PPase isoforms in Cucumis sativus under heavy metal stress
Katarzyna Kabala et al.
PHYSIOLOGIA PLANTARUM (2014)
An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore
Kambiz N. Alavian et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
The c ring of the F1Fo ATP synthase forms the mitochondrial permeability transition pore: a critical appraisal
Andrew P. Halestrap
FRONTIERS IN ONCOLOGY (2014)
Microscopy of single FoF1-ATP synthases The unraveling of motors, gears, and controls
Michael Boersch
IUBMB LIFE (2013)
The V-ATPase membrane domain is a sensor of granular pH that controls the exocytotic machinery
Sandrine Poea-Guyon et al.
JOURNAL OF CELL BIOLOGY (2013)
Autophagosomal Syntaxin 17-dependent lysosomal degradation maintains neuronal function in Drosophila
Szabolcs Takats et al.
JOURNAL OF CELL BIOLOGY (2013)
Mechanism of Cd and Cu action on the tonoplast proton pumps in cucumber roots
Katarzyna Kabala et al.
PHYSIOLOGIA PLANTARUM (2013)
The Hairpin-type Tail-Anchored SNARE Syntaxin 17 Targets to Autophagosomes for Fusion with Endosomes/Lysosomes
Eisuke Itakura et al.
CELL (2012)
Mediatophore regulates acetylcholine release from T cells
Takeshi Fujii et al.
JOURNAL OF NEUROIMMUNOLOGY (2012)
The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles
Bernd Strasser et al.
EMBO JOURNAL (2011)
A role for V-ATPase subunits in synaptic vesicle fusion?
Oussama El Far et al.
JOURNAL OF NEUROCHEMISTRY (2011)
V-ATPase Membrane Sector Associates with Synaptobrevin to Modulate Neurotransmitter Release
Jerome Di Giovanni et al.
NEURON (2010)
Exocytosis, Mediatophore, and Vesicular Ca2+/H+ Antiport in Rapid Neurotransmission
Yves Dunant et al.
MECHANISMS OF EXOCYTOSIS (2009)
A divalent-ion binding site on the 16-kDa proton channel from Nephrops norvegicus-revealed by EPR spectroscopy
Tibor Pali et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES (2006)
Interaction of inhibitors of the vacuolar H+-ATPase with the transmembrane Vo-sector
T Páli et al.
BIOCHEMISTRY (2004)
Expression of the acetylcholine release mechanism in various cells and reconstruction of the release mechanism in non-releasing cells
M Malo et al.
LIFE SCIENCES (2003)
Share Paper
