Title |
Probing Subunit-Subunit Interactions in the Yeast Vacuolar ATPase by Peptide Arrays
|
---|---|
Published in |
PLOS ONE, October 2012
|
DOI | 10.1371/journal.pone.0046960 |
Pubmed ID | |
Authors |
Lee S. Parsons, Stephan Wilkens |
Abstract |
Vacuolar (H(+))-ATPase (V-ATPase; V(1)V(o)-ATPase) is a large multisubunit enzyme complex found in the endomembrane system of all eukaryotic cells where its proton pumping action serves to acidify subcellular organelles. In the plasma membrane of certain specialized tissues, V-ATPase functions to pump protons from the cytoplasm into the extracellular space. The activity of the V-ATPase is regulated by a reversible dissociation mechanism that involves breaking and re-forming of protein-protein interactions in the V(1)-ATPase - V(o)-proton channel interface. The mechanism responsible for regulated V-ATPase dissociation is poorly understood, largely due to a lack of detailed knowledge of the molecular interactions that are responsible for the structural and functional link between the soluble ATPase and membrane bound proton channel domains. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 2 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 2 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United Kingdom | 2 | 8% |
United States | 2 | 8% |
Japan | 1 | 4% |
Unknown | 20 | 80% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 11 | 44% |
Student > Ph. D. Student | 6 | 24% |
Student > Bachelor | 2 | 8% |
Lecturer | 1 | 4% |
Other | 1 | 4% |
Other | 3 | 12% |
Unknown | 1 | 4% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 15 | 60% |
Biochemistry, Genetics and Molecular Biology | 6 | 24% |
Psychology | 1 | 4% |
Medicine and Dentistry | 1 | 4% |
Chemistry | 1 | 4% |
Other | 0 | 0% |
Unknown | 1 | 4% |