Results 1 to 10 of about 7,610 (197)

Regulation of proton-translocating V-ATPases [PDF]

open access: yesJournal of Experimental Biology, 1997
ABSTRACT Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning Vo domain.
H, Merzendorfer   +4 more
openaire   +4 more sources

The Importance of Vacuolar Ion Homeostasis and Trafficking in Hyphal Development and Virulence in Candida albicans

open access: yesFrontiers 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

Evolutionary primacy of sodium bioenergetics

open access: yesBiology 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

A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane [PDF]

open access: yes, 2008
Proteomic and phosphoproteomic analyses of rice shoot and root tonoplast-enriched and plasma membrane-enriched membrane fractions were carried out to look at tissue-specific expression, and to identify putative regulatory sites of membrane transport ...
Ahn   +38 more
core   +1 more source

The Presynaptic v-ATPase Reversibly Disassembles and Thereby Modulates Exocytosis but Is Not Part of the Fusion Machinery

open access: yesCell 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

Understanding the apparent stator-rotor connections in the rotary ATPase family using coarse-grained computer modeling [PDF]

open access: yes, 2014
Advances in structural biology, such as cryo-electron microscopy (cryo-EM) have allowed for a number of sophisticated protein complexes to be characterized.
Balakrishna   +40 more
core   +1 more source

Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states

open access: yeseLife, 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

Fluoride inhibition of proton-translocating ATPases of oral bacteria [PDF]

open access: yesInfection 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.
S V, Sutton, G R, Bender, R E, Marquis
openaire   +2 more sources

Cryo-EM studies of the rotary H+-ATPase/synthase from Thermus thermophilus

open access: yesBiophysics and Physicobiology, 2019
Proton-translocating rotary ATPases couple proton influx across the membrane domain and ATP hydrolysis/synthesis in the soluble domain through rotation of the central rotor axis against the surrounding peripheral stator apparatus.
Atsuko Nakanishi   +3 more
doaj   +1 more source

Intracellular proton pumps as targets in chemotherapy: V-ATPases and cancer [PDF]

open access: yes, 2012
Cancer cells show a metabolic shift that makes them overproduce protons; this has the potential to disturb the cellular acid-base homeostasis. However, these cells show cytoplasmic alkalinisation, increased acid
Hernández López, Agustín   +3 more
core   +1 more source

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