"Ca(2+) Mg(2+)-ATPase" 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.
An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3.
| Descriptor ID |
D017301
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| MeSH Number(s) |
D08.811.277.040.025.095
|
| Concept/Terms |
Ca(2+) Mg(2+)-ATPase- Ca(2+) Mg(2+)-ATPase
- Mg2+-ATPase
- Mg2+ ATPase
- Mg2+-Dependent ATPase
- ATPase, Mg2+-Dependent
- Mg2+ Dependent ATPase
- ATPase, Calcium Magnesium
- Calcium Magnesium ATPase
- Ca Mg-ATPase
- Ca Mg ATPase
- Ca2+-Mg2+ ATPase
- ATPase, Ca2+-Mg2+
- Ca2+ Mg2+ ATPase
- Adenosine Triphosphatase, Calcium, Magnesium
- Calcium Magnesium Adenosine Triphosphatase
- Adenosinetriphosphatase, Calcium, Magnesium
- Calcium Magnesium Adenosinetriphosphatase
- Adenosinetriphosphatase, Calcium Magnesium
- Adenosinetriphosphatase, Magnesium
- Magnesium Adenosinetriphosphatase
- Adenosine Triphosphatase, Magnesium
- Magnesium Adenosine Triphosphatase
- ATPase, Magnesium
- Magnesium ATPase
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Below are MeSH descriptors whose meaning is more general than "Ca(2+) Mg(2+)-ATPase".
Below are MeSH descriptors whose meaning is more specific than "Ca(2+) Mg(2+)-ATPase".
This graph shows the total number of publications written about "Ca(2+) Mg(2+)-ATPase" by people in this website by year, and whether "Ca(2+) Mg(2+)-ATPase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 0 | 1 | 1 |
| 1997 | 1 | 0 | 1 |
| 1999 | 0 | 1 | 1 |
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Below are the most recent publications written about "Ca(2+) Mg(2+)-ATPase" by people in Profiles.
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The N-terminal region of troponin T is essential for the maximal activation of rat cardiac myofilaments. J Mol Cell Cardiol. 1999 Apr; 31(4):867-80.
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Molecular and macromolecular specificity of human plasma phospholipid transfer protein. Biochemistry. 1997 Mar 25; 36(12):3645-53.
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Measurement of protein-protein interactions in reconstituted membrane vesicles using fluorescence spectroscopy. Methods Mol Biol. 1994; 27:95-100.
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The MgATPase activity of rat cardiac sarcoplasmic reticulum is a function of the calcium ATPase protein. Arch Biochem Biophys. 1992 Dec; 299(2):287-94.
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Ascorbate protects against tert-butyl hydroperoxide inhibition of erythrocyte membrane Ca2+ + Mg2(+)-ATPase. Arch Biochem Biophys. 1990 May 01; 278(2):416-24.
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The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker. Biochemistry. 1990 Mar 27; 29(12):3013-23.
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Hydroperoxides selectively inhibit human erythrocyte membrane enzymes. Arch Biochem Biophys. 1989 Sep; 273(2):527-34.
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Evidence for the association between two myosin heads in rigor acto-smooth muscle heavy meromyosin. Biochemistry. 1989 Feb 21; 28(4):1898-904.
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The inhibitory effects of polyoxyethylene detergents on human erythrocyte acetylcholinesterase and Ca2+ + Mg2+ ATPase. Biochem Cell Biol. 1989 Feb-Mar; 67(2-3):137-46.
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Two Ca2+-dependent ATPases in rat liver plasma membrane. The previously purified (Ca2+-Mg2+)-ATPase is not a Ca2+-pump but an ecto-ATPase. J Biol Chem. 1988 Sep 05; 263(25):12253-8.