H(+)-transporting V0 sector ATPase subunit a [Saccharomyces cerevisiae - Protein

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A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment. [J Biol Chem. 2018]
A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.
Hohlweg W, Wagner GE, Hofbauer HF, Sarkleti F, Setz M, Gubensäk N, Lichtenegger S, Falsone SF, Wolinski H, Kosol S, et al. J Biol Chem. 2018 Dec 7; 293(49):18977-18988. Epub 2018 Sep 12.
Structural analysis of the N-terminal domain of subunit a of the yeast vacuolar ATPase (V-ATPase) using accessibility of single cysteine substitutions to chemical modification. [J Biol Chem. 2013]
Structural analysis of the N-terminal domain of subunit a of the yeast vacuolar ATPase (V-ATPase) using accessibility of single cysteine substitutions to chemical modification.
Liberman R, Cotter K, Baleja JD, Forgac M. J Biol Chem. 2013 Aug 2; 288(31):22798-808. Epub 2013 Jun 5.
Topology, glycosylation and conformational changes in the membrane domain of the vacuolar H+-ATPase a subunit. [J Cell Biochem. 2013]
Topology, glycosylation and conformational changes in the membrane domain of the vacuolar H+-ATPase a subunit.
Kartner N, Yao Y, Bhargava A, Manolson MF. J Cell Biochem. 2013 Jul; 114(7):1474-87.

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