Vacuolar Proton-Translocating ATPases
"Vacuolar Proton-Translocating ATPases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Proton-translocating ATPases that are involved in acidification of a variety of intracellular compartments.
| Descriptor ID |
D025262
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| MeSH Number(s) |
D08.811.277.040.025.325.875 D08.811.913.696.650.150.500.875 D12.776.157.530.450.250.875.500.875 D12.776.543.585.450.250.875.500.875
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| Concept/Terms |
Vacuolar Proton-Translocating ATPases- Vacuolar Proton-Translocating ATPases
- Lysosomal Proton-Translocating ATPases
- ATPases, Lysosomal Proton-Translocating
- Lysosomal Proton Translocating ATPases
- Proton-Translocating ATPases, Lysosomal
- V-Type ATPase
- ATPase, V-Type
- V Type ATPase
- Vacuolar ATPase
- ATPase, Vacuolar
- Vacuolar F(1)F(0) ATPases
- Vacuolar H+-ATPase
- H+-ATPase, Vacuolar
- Vacuolar H+ ATPase
- Vacuolar Membrane H(+)-ATPase
- Lysosomal F(1)F(0) ATPase
- Vacuolar F(1)F(0) ATPase
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Below are MeSH descriptors whose meaning is more general than "Vacuolar Proton-Translocating ATPases".
Below are MeSH descriptors whose meaning is more specific than "Vacuolar Proton-Translocating ATPases".
This graph shows the total number of publications written about "Vacuolar Proton-Translocating ATPases" by people in this website by year, and whether "Vacuolar Proton-Translocating ATPases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 1 | 0 | 1 |
| 2004 | 1 | 0 | 1 |
| 2005 | 1 | 0 | 1 |
| 2010 | 1 | 0 | 1 |
| 2011 | 1 | 0 | 1 |
| 2012 | 2 | 0 | 2 |
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Below are the most recent publications written about "Vacuolar Proton-Translocating ATPases" by people in Profiles.
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Yuzlenko O, Lazaridis T. Membrane protein native state discrimination by implicit membrane models. J Comput Chem. 2013 Apr 05; 34(9):731-8.
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Hildenbrand ZL, Molugu SK, Bernal RA. Anchoring and scaffolding: V(1)-ATPase interactions with widespread implications. Cell Cycle. 2012 Jun 01; 11(11):2041-2.
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Zhou M, Morgner N, Barrera NP, Politis A, Isaacson SC, Matak-Vinkovic D, Murata T, Bernal RA, Stock D, Robinson CV. Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding. Science. 2011 Oct 21; 334(6054):380-385.
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Hildenbrand ZL, Molugu SK, Stock D, Bernal RA. The C-H peripheral stalk base: a novel component in V1-ATPase assembly. PLoS One. 2010 Sep 03; 5(9):e12588.
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De Mello WC. On the pathophysiological implications of an intracellular renin receptor. Circ Res. 2006 Dec 08; 99(12):1285-6.
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Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S. Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus. EMBO J. 2005 Nov 16; 24(22):3974-83.
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Bernal RA, Stock D. Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy. Structure. 2004 Oct; 12(10):1789-98.
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Davies L, Farrar NA, Satre M, Dottin RP, Gross JD. Vacuolar H(+)-ATPase and weak base action in Dictyostelium. Mol Microbiol. 1996 Oct; 22(1):119-26.