Results 141 to 150 of about 3,484 (169)

The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis. [PDF]

Biophys J
Macdonald JE, Ashby PD.
europepmc   +1 more source

Oxr1 and Ncoa7 regulate V-ATPase to achieve optimal pH for glycosylation within the Golgi apparatus and trans-Golgi network. [PDF]

Proc Natl Acad Sci U S A
Yoshimura SI, Sobajima T, Kunii M, Harada A.   +3 more
europepmc   +1 more source

A nanobody against the V-ATPase c subunit inhibits metastasis of 4T1-12B breast tumor cells to lung in mice. [PDF]

Oncotarget
Li Z, Alshagawi MA, Oot RA, Alamoudi MK, Su K, Li W, Collins MP, Wilkens S, Forgac M.   +8 more
europepmc   +1 more source

Na⁺ Translocation Dominates over H⁺-Translocation in the Membrane Pyrophosphatase with Dual Transport Specificity. [PDF]

Int J Mol Sci
Bogachev AV, Anashkin VA, Bertsova YV, Zavyalova EG, Baykov AA.   +4 more
europepmc   +1 more source

Arabidopsis COP1 guides stomatal response in guard cells through pH regulation. [PDF]

Commun Biol
Cha S, Min WK, Seo HS.
europepmc   +1 more source

Structures of rotary ATP synthase from <i>Thermus thermophilus</i> during proton powered ATP synthesis. [PDF]

Sci Adv
Nakano A, Kishikawa JI, Yui N, Sugawara K, Kan Y, Gerle C, Shigematsu H, Mitsuoka K, Yokoyama K.   +8 more
europepmc   +1 more source

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.
P M, Kane, T H, Stevens
openaire   +4 more sources

Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase

Biochemistry, 1996
In order to generate a set of tools for probing structure-function relationships in the catalytic subunit of the yeast vacuolar H(+)-ATPase, the gene encoding this subunit (VMA1) was randomly mutagenized. Mutant plasmids unable to complement the growth defects of yeast cells lacking an intact VMA1 gene were isolated and sequenced.
J, Liu, P M, Kane
openaire   +2 more sources

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).
G H, Sun-Wada, H, Murakami, H, Nakai, Y, Wada, M, Futai   +4 more
openaire   +2 more sources

Protein sorting in yeast: the role of the vacuolar protontranslocating ATPase

Journal of Cell Science, 1989
ABSTRACT We are investigating the physiological roles of organelle acidification in yeast by two different approaches. First, we have identified two mutants which are defective in acidification of the yeast lysosome-like vacuole from among a collection of mutants which mis-sort soluble vacuolar proteins to the cell surface. These mutants
P M, Kane, C T, Yamashiro, J H, Rothman, T H, Stevens   +3 more
openaire   +2 more sources