Results 41 to 50 of about 10,440,305 (287)
The curious case of vacuolar ATPase: regulation of signaling pathways
The Vacuolar ATPase (V-ATPase) is a proton pump responsible for controlling the intracellular and extracellular pH of cells. The structure of V-ATPase has been highly conserved among all eukaryotic cells and is involved in diverse functions across ...
Sahithi Pamarthy +3 more
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Loss of the V-ATPase B1 subunit isoform expressed in non-neuronal cells of the mouse olfactory epithelium impairs olfactory function. [PDF]
The vacuolar proton-pumping ATPase (V-ATPase) is the main mediator of intracellular organelle acidification and also regulates transmembrane proton (H(+)) secretion, which is necessary for an array of physiological functions fulfilled by organs such as ...
Teodor G Păunescu +6 more
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Objective: The diabetic heart is characterized by extensive lipid accumulation which often leads to cardiac contractile dysfunction. The underlying mechanism involves a pivotal role for vacuolar-type H+-ATPase (v-ATPase, functioning as endosomal ...
Shujin Wang +11 more
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Immunolocalization of IP3R and V-ATPase in Ameloblastomas [PDF]
The goal of this study was to investigate the immunolocalization of inositol 1,4,5-trisphosphate receptor (IP3R) and vacuolar ATPase (V-ATPase) in ameloblastomas with special attention to the invasive front. Thirty-seven cases of previously diagnosed formalin-fixed paraffin-embedded (FFPE) human ameloblastoma samples were selected for this study.
Allan Fernando Giovanini +7 more
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Defining steps in RAVE-catalyzed V-ATPase assembly using purified RAVE and V-ATPase subcomplexes [PDF]
The vacuolar H+-ATPase (V-ATPase) is a highly conserved proton pump responsible for the acidification of intracellular organelles in virtually all eukaryotic cells. V-ATPases are regulated by the rapid and reversible disassembly of the peripheral V1 domain from the integral membrane Vo domain, accompanied by release of the V1 C subunit from both ...
Michael C. Jaskolka +4 more
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The illustration of V-ATPase and ECDD-S16 interaction.
(A) Image depicts the binding between ECDD-S16 and V-ATPase V0 region. (B) A close-up view of the binding pocket between V-ATPase and ECDD-S16 illustrates the location of neighboring amino acids around ECDD-S16.
Napason Chabang (17457772) +14 more
core +1 more source
HCO3−-independent pH Regulation in Astrocytes in Situ Is Dominated by V-ATPase
The mechanisms of HCO3−-independent intracellular pH (pHi) regulation were examined in fibrous astrocytes within isolated neonatal rat optic nerve (RON) and in cultured cortical astrocytes.
R. Fern (7680761) +3 more
core +3 more sources
RNA Interference of Genes Encoding the Vacuolar-ATPase in Liriomyza trifolii
The leafminer fly, Liriomyza trifolii, is an invasive pest of vegetable and horticultural crops in China. In this study, a microinjection method based on dsRNA was developed for RNA interference (RNAi) in L. trifolii using genes encoding vacuolar-ATPase (
Ya-Wen Chang +4 more
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Regulation of proton-translocating V-ATPases [PDF]
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 +2 more sources
Vacuolar ATPase as a potential therapeutic target and mediator of treatment resistance in cancer
Vacuolar ATPase (V‐ATPase) is an ATP‐dependent H+‐transporter that pumps protons across intracellular and plasma membranes. It consists of a large multi‐subunit protein complex and influences a wide range of cellular processes.
Bradleigh Whitton +3 more
doaj +1 more source

