Results 11 to 20 of about 3,484 (169)

Regulation of Vacuolar Proton-translocating ATPase Activity and Assembly by Extracellular pH [PDF]

Journal of Biological Chemistry, 2010
Vacuolar proton-translocating ATPases (V-ATPases) are responsible for organelle acidification in all eukaryotic cells. The yeast V-ATPase, known to be regulated by reversible disassembly in response to glucose deprivation, was recently reported to be regulated by extracellular pH as well (Padilla-López, S., and Pearce, D. A. (2006) J. Biol. Chem.
Theodore T, Diakov, Patricia M, Kane
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Cloning of Entamoeba genes encoding proteolipids of putative vacuolar proton-translocating ATPases [PDF]

Infection and Immunity, 1994
Molecular cloning techniques were used to identify genes encoding the proteolipids of putative vacuolar proton-transporting ATPases (V-ATPases; EC 3.6.1.35) of Entamoeba histolytica (Ehvma3) and Entamoeba dispar. The Ehvma3 gene encoded a 177-amino-acid peptide, with an M(r) of 18,110, which showed extensive positional identities with peptides of E ...
S, Descoteaux, Y, Yu, J, Samuelson
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Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry [PDF]

Analytical Biochemistry, 2010
Fluorescence intensity of the pH-sensitive carboxyfluorescein derivative 2,7-bis(2-carboxyethyl)-5(6)-carboxyfluorescein (BCECF) was monitored by high-throughput flow cytometry in living yeast cells. We measured fluorescence intensity of BCECF trapped in yeast vacuoles, acidic compartments equivalent to lysosomes where vacuolar proton-translocating ...
Rebecca M, Johnson, Chris, Allen, Sandra D, Melman, Anna, Waller, Susan M, Young, Larry A, Sklar, Karlett J, Parra   +6 more
openaire   +4 more sources

Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase) [PDF]

Journal of Biological Chemistry, 2012
Vacuolar proton-translocating ATPase (V-ATPase) is a central regulator of cellular pH homeostasis, and inactivation of all V-ATPase function has been shown to prevent infectivity in Candida albicans. V-ATPase subunit a of the Vo domain (Voa) is present as two fungal isoforms: Stv1p (Golgi) and Vph1p (vacuole).
Gregory C. Finnigan, Glen E. Cronan, Hae J. Park, Sankaranarayanan Srinivasan, Florante A. Quiocho, Tom H. Stevens   +5 more
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V1-situated Stalk Subunits of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
The proton-translocating ATPase of the yeast vacuole is an enzyme complex consisting of a large peripheral membrane sector (V1) and an integral membrane sector (V0), each composed of multiple subunits. The V1 sector contains subunits that hydrolyze ATP, whereas the V0 sector contains subunits that translocate protons across the membrane.
J J, Tomashek, L A, Graham, M U, Hutchins, T H, Stevens, D J, Klionsky   +4 more
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The role of the host—Neutrophil biology

Periodontology 2000, EarlyView., 2023
Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple, Josefine Hirschfeld, Alpdogan Kantarci, Asaf Wilensky, Lior Shapira   +4 more
wiley   +1 more source

Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy [PDF]

Frontiers in Pharmacology, 2014
Vacuolar proton-translocating ATPase (V-ATPase) is a membrane-bound, multi-subunit enzyme that uses the energy of ATP hydrolysis to pump protons across membranes. V-ATPase activity is critical for pH homeostasis and organelle acidification as well as for generation of the membrane potential that drives secondary transporters and cellular metabolism.
Summer R. Hayek, Samuel A. Lee, Samuel A. Lee, Karlett J. Parra   +3 more
openaire   +3 more sources

Conformation of a Peptide Encompassing the Proton Translocation Channel of Vacuolar H+-ATPase [PDF]

Biophysical Journal, 2007
The structural properties of a crucial transmembrane helix for proton translocation in vacuolar ATPase are studied using double site-directed spin-labeling combined with electron spin resonance (ESR) (or electron paramagnetic resonance) and circular dichroism spectroscopy in sodium dodecyl sulfate micelles.
Vos, W.L., Vermeer, L.S., Hemminga, M.A.
openaire   +3 more sources

Loss of Vacuolar Proton-translocating ATPase Activity in Yeast Results in Chronic Oxidative Stress [PDF]

Journal of Biological Chemistry, 2007
Yeast mutants lacking vacuolar proton-translocating ATPase (V-ATPase) subunits (vma mutants) were sensitive to several different oxidants in a recent genomic screen (Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 6564-6569). We confirmed that mutants lacking a V(1) subunit (vma2Delta),
Elena, Milgrom, Heba, Diab, Frank, Middleton, Patricia M, Kane   +3 more
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Reconstitution in Vitro of the V1 Complex from the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
Oligomeric assembly is a fundamental aspect of many complex enzymes. Using our native gel technique for examining subcomplexes of the V-ATPase V1 sector, we have developed an in vitro reconstitution assay for assembly of this complex. Assembly of complex II, the soluble V1 complex observed in native gels, is dependent upon the presence of divalent ...
John J. Tomashek, Brian S. Garrison, Daniel J. Klionsky   +2 more
openaire   +2 more sources