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ATP Synthase Members of Chloroplasts and Mitochondria in Rubber Trees (Hevea brasiliensis) Response to Plant Hormones [PDF]

open access: yesPlants
ATP synthase is a key enzyme in photophosphorylation in photosynthesis and oxidative phosphorylation in respiration, which can catalyze the synthesis of ATP and supply energy to organisms. ATP synthase has been well studied in many animal species but has
Bingbing Guo   +5 more
doaj   +2 more sources

An overview of ATP synthase, inhibitors, and their toxicity [PDF]

open access: yesHeliyon, 2023
Mitochondrial complex V (ATP synthase) is a remarkable molecular motor crucial in generating ATP and sustaining mitochondrial function. Its importance in cellular metabolism cannot be overstated, as malfunction of ATP synthase has been linked to various ...
Arwa R. Althaher, Mohammad Alwahsh
doaj   +2 more sources

Targeting the ATP Synthase in Staphylococcus aureus Small Colony Variants, Streptococcus pyogenes and Pathogenic Fungi

open access: yesAntibiotics, 2021
The ATP synthase has been validated as a druggable target with the approval of the ATP synthase inhibitor, bedaquiline, for treatment of drug-resistant Mycobacterium tuberculosis, a bacterial species in which the ATP synthase is essential for viability ...
Martin Vestergaard   +2 more
doaj   +1 more source

Autoantibodies to endothelial cell surface ATP synthase, the endogenous receptor for hsp60, might play a pathogenic role in vasculatides. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: Heat shock protein (hsp) 60 that provides "danger signal" binds to the surface of resting endothelial cells (EC) but its receptor has not yet been characterized. In mitochondria, hsp60 specifically associates with adenosine triphosphate (ATP)
Jean-Eric Alard   +6 more
doaj   +1 more source

IF1 promotes oligomeric assemblies of sluggish ATP synthase and outlines the heterogeneity of the mitochondrial membrane potential

open access: yesCommunications Biology, 2023
The coexistence of two pools of ATP synthase in mitochondria has been largely neglected despite in vitro indications for the existence of reversible active/inactive state transitions in the F1-domain of the enzyme.
Inés Romero-Carramiñana   +4 more
doaj   +1 more source

Inhibitors of ATP Synthase as New Antibacterial Candidates

open access: yesAntibiotics, 2023
ATP, the power of all cellular functions, is constantly used and produced by cells. The enzyme called ATP synthase is the energy factory in all cells, which produces ATP by adding inorganic phosphate (Pi) to ADP.
Rawan Mackieh   +5 more
doaj   +1 more source

Human F1F0 ATP synthase, mitochondrial ultrastructure and OXPHOS impairment: a (super-)complex matter? [PDF]

open access: yesPLoS ONE, 2013
Mitochondrial morphogenesis is a key process of cell physiology. It is essential for the proper function of this double membrane-delimited organelle, as it ensures the packing of the inner membrane in a very ordered pattern called cristae.
Johann Habersetzer   +6 more
doaj   +1 more source

ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast

open access: yesScientific Reports, 2023
The mitochondrial ATP synthase, an enzyme that synthesizes ATP and is involved in the formation of the mitochondrial mega-channel and permeability transition, is a multi-subunit complex. In S.
Chiranjit Panja   +4 more
doaj   +1 more source

Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca2+-Dependent Formation of Large Channels

open access: yesCells, 2023
Monomers, dimers, and individual FOF1-ATP synthase subunits are, presumably, involved in the formation of the mitochondrial permeability transition pore (PTP), whose molecular structure, however, is still unknown.
Anna B. Nikiforova   +8 more
doaj   +1 more source

ATP synthase-associated coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing proteins are critical for mitochondrial function in Toxoplasma gondii

open access: yesmBio, 2023
Coiled-coil-helix-coiled-coil-helix (CHCH) domains consist of two pairs of cysteine residues that are oxidized to form disulfide bonds upon mitochondrial import.
Madelaine M. Usey, Diego Huet
doaj   +1 more source

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