Antifungal mechanism of action of lactoferrin: Identification of H+-ATPase (P3A-type) as a new apoptotic-cell membrane receptor [PDF]
Human lactoferrin (hLf) is a protein of the innate immune system which induces an apoptotic-like process in yeast. Determination of the susceptibility to lactoferrin of several yeast species under different metabolic conditions, respiratory activity ...
Acosta Zaldívar, Maikel +2 more
core +1 more source
Computational modeling of TC0583 as a putative component of the Chlamydia muridarum V-type ATP synthase complex and assessment of its protective capabilities as a vaccine antigen. [PDF]
Numerous Chlamydia trachomatis proteins have been identified as potential subunit vaccines, of which the major outer-membrane protein (MOMP) has, so far, proven the most efficacious. Recently, subunit A of the V-type ATP synthase (ATPase; TC0582) complex
Barta, Michael L +4 more
core +1 more source
Proton-translocating ATPase and lysosomal cystine transport.
A proton-translocating ATPase was identified in highly purified lysosomes from Epstein-Barr virus-transformed human lymphoblasts. Activity of this ATPase caused acidification of highly purified, fluorescein isothiocyanate dextran-loaded lysosomes and correlated with the ATP-dependent efflux of lysosomal cystine.
A J, Jonas +5 more
openaire +2 more sources
Proton-translocating Mg2+-dependent ATPase activity in insulin-secretory granules [PDF]
Insulin-secretory granules isolated from a pancreatic islet-cell tumour by centrifugation on Percoll density gradients exhibited a membrane-associated Mg2+-dependent ATPase activity. In granule suspensions incubated in iso-osmotic media, activity was increased 2–3-fold by carbonyl cyanide p-trifluoromethoxyphenylhydrazone, the combination of ...
J C, Hutton, M, Peshavaria
openaire +2 more sources
Subcellular distribution of the V-ATPase complex in plant cells, and localisation of the 100 kDa subunit VHA-a within the complex [PDF]
Background Vacuolar H+-ATPases are large protein complexes of more than 700 kDa that acidify endomembrane compartments and are part of the secretory system of eukaryotic cells. They are built from 14 different (VHA)-subunits.
Kluge Christoph +9 more
core +3 more sources
Kinetic analysis of proton translocation catalyzed by F0F1 ATPase [PDF]
Kinetic analysis of both proton translocating and steady‐state ATP hydrolytic activities catalyzed by F0F1 ATPase in submitochondrial particles were carried out over an ATP concentration range of 1–2000 μM. The results were examined in relation to the prediction based on the alternate binding change model proposed by Gresser et al. [(1982) J.
Muneyuki, Eiro, Hirata, Hajime
openaire +2 more sources
Bacteria‐Responsive Nanostructured Drug Delivery Systems for Targeted Antimicrobial Therapy
Bacteria‐responsive nanocarriers are designed to release antimicrobials only in the presence of infection‐specific cues. This selective activation ensures drug release precisely at the site of infection, avoiding premature or indiscriminate release, and enhancing efficacy.
Guillermo Landa +3 more
wiley +1 more source
Regulatory assembly of the vacuolar proton pump VOV1-ATPase in yeast cells by FLIM-FRET
We investigate the reversible disassembly of VOV1-ATPase in life yeast cells by time resolved confocal FRET imaging. VOV1-ATPase in the vacuolar membrane pumps protons from the cytosol into the vacuole. VOV1-ATPase is a rotary biological nanomotor driven
Batisse, Claire +4 more
core +1 more source
We report a new thiolate‐reactive α,α‐gem‐dibromo lactam warhead that activates transcription factor Nrf2 and demonstrates anti‐inflammatory activities, which have implications in cancer, neurodegeneration, and cardiovascular diseases. RNA‐seq illuminated detailed transcriptional profiles, and chemical reactions with cysteine‐containing compounds ...
Beau R. Brummel +16 more
wiley +1 more source
Structure of the novel membrane-coating material in proton-secreting epithelial cells and identification as an H+ATPase. [PDF]
Specialized proton-secreting cells known collectively as mitochondria-rich cells are found in a variety of transporting epithelia, including the kidney collecting duct (intercalated cells) and toad and turtle urinary bladders.
Brown, D, Gluck, S, Hartwig, J
core

