Results 21 to 30 of about 147,751 (260)

Wheat V-H+-ATPase subunit genes significantly affect salt tolerance in Arabidopsis thaliana. [PDF]

PLoS ONE, 2014
Genes for V-H(+)-ATPase subunits were identified and cloned from the salt-tolerant wheat mutant RH8706-49. Sequences of these genes are highly conserved in plants.
Xiaoliang He, Xi Huang, Yinzhu Shen, Zhanjing Huang   +3 more
doaj   +1 more source

SNARE, V-ATPase et neurotransmission [PDF]

médecine/sciences, 2011
> La communication entre neurones repose principalement sur les synapses chimiques et par consequent sur la liberation de neurotransmetteurs. Au niveau des terminaisons nerveuses, des vesicules synaptiques remplies de neurotransmetteurs s’arriment a la membrane plasmique et subissent des etapes de maturation qui les rendent competentes pour la fusion ...
El Far, Oussama, Seagar, Michael
openaire   +2 more sources

The role of individual domains and the significance of shedding of ATP6AP2/(pro)renin receptor in vacuolar H(+)-ATPase biogenesis.

PLoS ONE, 2013
The ATPase 6 accessory protein 2 (ATP6AP2)/(pro)renin receptor (PRR) is essential for the biogenesis of active vacuolar H(+)-ATPase (V-ATPase). Genetic deletion of ATP6AP2/PRR causes V-ATPase dysfunction and compromises vesicular acidification.
Kenichiro Kinouchi, Atsuhiro Ichihara, Motoaki Sano, Ge-Hong Sun-Wada, Yoh Wada, Hiroki Ochi, Toru Fukuda, Kanako Bokuda, Hideaki Kurosawa, Naohiro Yoshida, Shu Takeda, Keiichi Fukuda, Hiroshi Itoh   +12 more
doaj   +1 more source

V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis

Theranostics, 2018
Vacuolar ATPases (V-ATPases) play a critical role in regulating extracellular acidification of osteoclasts and bone resorption. The deficiencies of subunit a3 and d2 of V-ATPases result in increased bone density in humans and mice. One of the traditional drug design strategies in treating osteoporosis is the use of subunit a3 inhibitor. Recent findings
Duan, Xiaohong, Yang, Shaoqing, Zhang, Lei, Yang, Tielin   +3 more
openaire   +2 more sources

Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2016
V-ATPases are ATP-driven proton pumps that function within both intracellular compartments and the plasma membrane in a wide array of normal physiological and pathophysiological processes. V-ATPases are composed of a peripheral V(1) domain that hydrolyzes ATP and an integral V(0) domain that transports protons.
Christina, McGuire, Kristina, Cotter, Laura, Stransky, Michael, Forgac   +3 more
openaire   +3 more sources

Regulation of V-ATPase activity

Frontiers in Bioscience, 2017
V-ATPases are ATP-driven proton pumps present in both intracellular and cell surface membranes of eukaryotes that function in many normal and disease processes. V-ATPases are large, multi-subunit complexes composed of a peripheral domain (V1) that hydrolyzes ATP and a membrane integral domain (V0) that translocates protons.
Christina, McGuire, Laura, Stransky, Kristina, Cotter, Michael, Forgac   +3 more
openaire   +2 more sources

V-ATPase engagement in autophagic processes [PDF]

Autophagy, 2011
The proton pumping activity of V-ATPase is responsible for acidification of the lysosome/vacuole. The low lumenal pH of this organelle stimulates the activity of a battery of resident hydrolases responsible for the degradation of various nonselective and selective cargos delivered by autophagic processes.
Dalibor, Mijaljica, Mark, Prescott, Rodney J, Devenish   +2 more
openaire   +2 more sources

An extended nomenclature for mammalian V-ATPase subunit genes and splice variants. [PDF]

PLoS ONE, 2010
The vacuolar-type H(+)-ATPase (V-ATPase) is a multisubunit proton pump that is involved in both intra- and extracellular acidification processes throughout the body.
Kevin C Miranda, Fiona E Karet, Dennis Brown   +2 more
doaj   +1 more source

Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. [PDF]

PLoS ONE, 2010
BackgroundThe vacuolar H+-ATPase, or V-ATPase, is a highly-conserved multi-subunit enzyme that transports protons across membranes at the expense of ATP.
Margaret Clarke, Lucinda Maddera, Ulrike Engel, Günther Gerisch   +3 more
doaj   +1 more source

Regulation and Isoform Function of the V-ATPases [PDF]

Biochemistry, 2010
The vacuolar (H(+))-ATPases are ATP-dependent proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane of eukaryotic cells. Intracellular V-ATPases play an important role in normal physiological processes such as receptor-mediated endocytosis, intracellular membrane trafficking, pro-hormone ...
Masashi, Toei, Regina, Saum, Michael, Forgac   +2 more
openaire   +2 more sources