Results 31 to 40 of about 147,751 (260)

F-actin reorganization by V-ATPase inhibition in prostate cancer

open access: yesBiology Open, 2017
The vacuolar ATPase (V-ATPase) proton pump sustains cellular pH homeostasis, and its inhibition triggers numerous stress responses. However, the cellular mechanisms involved remain largely elusive in cancer cells.
Yamhilette Licon-Munoz   +3 more
doaj   +1 more source

Specific amino acid supplementation rescues the heart from lipid overload-induced insulin resistance and contractile dysfunction by targeting the endosomal mTOR–v-ATPase axis

open access: yesMolecular Metabolism, 2021
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
doaj   +1 more source

Defining steps in RAVE-catalyzed V-ATPase assembly using purified RAVE and V-ATPase subcomplexes [PDF]

open access: yesJournal of Biological Chemistry, 2021
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
openaire   +2 more sources

The curious case of vacuolar ATPase: regulation of signaling pathways

open access: yesMolecular Cancer, 2018
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
doaj   +1 more source

Loss of the V-ATPase B1 subunit isoform expressed in non-neuronal cells of the mouse olfactory epithelium impairs olfactory function. [PDF]

open access: yesPLoS ONE, 2012
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
doaj   +1 more source

Immunolocalization of IP3R and V-ATPase in Ameloblastomas [PDF]

open access: yesHead and Neck Pathology, 2019
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
openaire   +2 more sources

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   +2 more sources

RNA Interference of Genes Encoding the Vacuolar-ATPase in Liriomyza trifolii

open access: yesInsects, 2021
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
doaj   +1 more source

Vacuolar ATPase as a potential therapeutic target and mediator of treatment resistance in cancer

open access: yesCancer Medicine, 2018
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

CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7

open access: yesLife Science Alliance, 2022
The structure of mammalian V-ATPase with mEAK-7 shows how a TLDc domain-containing protein can bind the proton pump to form an activity-sensitive interaction.
Yong Zi Tan   +10 more
doaj   +1 more source

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