Results 11 to 20 of about 5,151 (179)
Functional and structural characterization of F1‐ATPase with common ancestral core domains in stator ring [PDF]
Protein Science, Volume 34, Issue 11, November 2025.Abstract Extant F1‐ATPases exhibit diverse rotational stepping behaviors—3‐, 6‐, or 9‐step cycles—yet the evolutionary origin of these patterns remains unclear. Here, we used ancestral sequence reconstruction to infer the catalytic β and non‐catalytic α subunits of a putative ancestral F1‐ATPase.
Aya K. Suzuki +7 more
wiley +2 more sources
Frontiers in Microbiology, 2021 The vacuole of Candida albicans plays a significant role in many processes including homeostasis control, cellular trafficking, dimorphic switching, and stress tolerance.
Quanzhen Lv, Lan Yan, Yuanying Jiang
doaj +1 more source
Localization of a Proton-Translocating ATPase on Sucrose Gradients [PDF]
Plant Physiology, 1982 Ionophore-stimulated ATPase activity and ATP-dependent quinacrine quench were enriched in parallel when microsomal vesicles were prepared from corn (Crow Single Cross Hybrid WF9-Mo17) roots and collected on a cushion of 10% dextran. Activities were highest in the apical 1.5 centimeters of the roots.
Frances M. DuPont +2 more
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Electrogenic Proton Translocation by the ATPase of Sugarcane Vacuoles [PDF]
Plant Physiology, 1985 Existence of a proton-translocating ATPase on the tonoplast of higher plants has been further confirmed by use of two experimental systems: (a) intact isolated vacuoles from sugarcane cells and (b) vesicles prepared from the same source. Addition of MgATP to vacuoles polarized the tonoplast by 40 millivolts to a value of +20 millivolts, but a large ...
Margaret Thom, Ewald Komor
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Proton translocation driven by ATP hydrolysis in V‐ATPases [PDF]
FEBS Letters, 2003 The vacuolar H+‐ATPases (or V‐ATPases) are a family of ATP‐dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubunit complexes composed of a peripheral domain (V1) responsible for ATP hydrolysis and an integral domain ...
Tsuyoshi Nishi +2 more
openaire +2 more sources
Evolutionary primacy of sodium bioenergetics
Biology Direct, 2008 Background The F- and V-type ATPases are rotary molecular machines that couple translocation of protons or sodium ions across the membrane to the synthesis or hydrolysis of ATP.
Wolf Yuri I +4 more
doaj +1 more source
Fluoride inhibition of proton-translocating ATPases of oral bacteria [PDF]
Infection and Immunity, 1987 The ATPases of isolated membranes of lactic acid bacteria were found to be inhibited by fluoride in a complex manner. Among the enzymes tested, that of Streptococcus mutans GS-5 was the most sensitive to fluoride, and the initial rate of hydrolysis of ATP was reduced 50% by approximately 3 mM fluoride.
G. R. Bender +2 more
openaire +3 more sources
Cell Reports, 2017 Vacuolar H+-ATPase (v-ATPase) is a multi-subunit complex comprising two domains: the cytosolic V1 domain catalyzing ATP hydrolysis and the membranous V0 sector translocating protons across membranes.
Anna Bodzęta +2 more
doaj +1 more source
Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states
eLife, 2016 A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy.
Meghna Sobti +6 more
doaj +1 more source
Proton translocation induced by ATPase activity in chloroplasts [PDF]
FEBS Letters, 1970 Proton uptake by chloroplasts was induced by light‐triggered ATPase activity. A quotient of two was obtained when the initial rate of proton uptake was divided by the rate of Pi released from ATP. Gramicidin accelerated the rate of ATPase activity and reduced the H+/Pi ratio to 1.4. The results were found to be consistent with the chemiosmotic theory.
openaire +3 more sources