Results 91 to 100 of about 2,277 (122)

Vacuolar-ATPase inhibitors are antimicrobial agents active against intracellular mycobacteria. [PDF]

open access: yesAntimicrob Agents Chemother
Rankine-Wilson L   +9 more
europepmc   +1 more source

V-ATPase-dependent induction of selective autophagy. [PDF]

open access: yesNat Commun
Huang Y   +5 more
europepmc   +1 more source

MiR-92 Controls Synaptic Development Through Glial Vha55 Regulation. [PDF]

open access: yesBiomolecules
Moe SM   +4 more
europepmc   +1 more source

Mycobacterium tuberculosis modulates phosphorylation of host ATP6V1E1 to promote intracellular survival. [PDF]

open access: yesNat Commun
Chen J   +22 more
europepmc   +1 more source

Mouse Atp6f, the gene encoding the 23-kDa proteolipid of vacuolar proton translocating ATPase

Gene, 2001
The 23-kDa proteolipid subunit of mouse vacuolar-type proton-translocating ATPase (V-ATPase) was predicted to be a hydrophobic polypeptide of 205 amino acid residues with five putative transmembrane segments. It exhibits sequence similarity to Vma16p of Saccharomyces cerevisiae and vha-4 of Caenorhabdittis elegans (83 and 84%, respectively).
Hiroyuki Nakai   +2 more
exaly   +3 more sources

Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase

Journal of Bioenergetics and Biomembranes, 1992
The yeast vacuole is acidified by a vacuolar proton-translocating ATPase (H(+)-ATPase) that closely resembles the vacuolar H(+)-ATPases of other fungi, animals, and plants. The yeast enzyme is purified as a complex of eight subunits, which include both integral and peripheral membrane proteins.
Tom Stevens   +2 more
exaly   +3 more sources

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