The DOI matches its Crossref record; 136 of the 136 references it cites were found in a registry or an index.
The vacuolar H+-ATPase: a universal proton pump of eukaryotes
Open accessAbstract
The vacuolar H+-ATPase (V-ATPase) is a universal component of eukaryotic organisms. It is present in the membranes of many organelles, where its proton-pumping action creates the low intra-vacuolar pH found, for example, in lysosomes. In addition, there are a number of differentiated cell types that have V-ATPases on their surface that contribute to the physiological functions of these cells. The V-ATPase is a multi-subunit enzyme composed of a membrane sector and a cytosolic catalytic sector. It is related to the familiar FoF1 ATP synthase (F-ATPase), having the same basic architectural construction, and many of the subunits from the two display identity with one another. All the core subunits of the V-ATPase have now been identified and much is known about the assembly, regulation and pharmacology of the enzyme. Recent genetic analysis has shown the V-ATPase to be a vital component of higher eukaryotes. At least one of the subunits, i.e. subunit c (ductin), may have multifunctional roles in membrane transport, providing a possible pathway of communication between cells. The structure of the membrane sector is known in some detail, and it is possible to begin to suggest how proton pumping is coupled to ATP hydrolysis.
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Cites
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Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles
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Selective Induction of Apoptosis with Proton Pump Inhibitor in Gastric Cancer Cells
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Metadata
- Authors
- FINBOW, M. E., & HARRISON, M. A.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-06-15
- Volume
- 324
- Issue
- 3
- Pages
- 697-712
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1833122216
- Cited by
- 269
- References
- 136
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- green
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