 Adenosine Triphosphatases
"Adenosine Triphosphatases" 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.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
| Descriptor ID |
D000251
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| MeSH Number(s) |
D08.811.277.040.025
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| Concept/Terms |
DNA-Dependent Adenosinetriphosphatases- DNA-Dependent Adenosinetriphosphatases
- Adenosinetriphosphatases, DNA-Dependent
- DNA Dependent Adenosinetriphosphatases
- ATPase, DNA-Dependent
- ATPase, DNA Dependent
- DNA-Dependent ATPase
- DNA Dependent ATPase
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Below are MeSH descriptors whose meaning is more general than "Adenosine Triphosphatases".
Below are MeSH descriptors whose meaning is more specific than "Adenosine Triphosphatases".
This graph shows the total number of publications written about "Adenosine Triphosphatases" by people in this website by year, and whether "Adenosine Triphosphatases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1993 | 0 | 1 | 1 | | 1995 | 0 | 1 | 1 | | 1996 | 0 | 1 | 1 | | 1998 | 2 | 0 | 2 | | 1999 | 0 | 2 | 2 | | 2000 | 0 | 1 | 1 | | 2001 | 0 | 1 | 1 | | 2002 | 1 | 1 | 2 | | 2003 | 0 | 1 | 1 | | 2004 | 0 | 2 | 2 | | 2005 | 0 | 3 | 3 | | 2010 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2012 | 1 | 0 | 1 | | 2013 | 1 | 0 | 1 |
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Below are the most recent publications written about "Adenosine Triphosphatases" by people in Profiles.
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Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science. 2013 Mar 01; 339(6123):1080-3.
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Wang Y, Gibney PA, West JD, Morano KA. The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds. Mol Biol Cell. 2012 Sep; 23(17):3290-8.
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Helsen CW, Glover JR. Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem. 2012 Jan 02; 287(1):542-56.
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Sun W, Vida TA, Sirisaengtaksin N, Merrill SA, Hanson PI, Bean AJ. Cell-free reconstitution of multivesicular body formation and receptor sorting. Traffic. 2010 Jun; 11(6):867-76.
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Kohn H, Widger W. The molecular basis for the mode of action of bicyclomycin. Curr Drug Targets Infect Disord. 2005 Sep; 5(3):273-95.
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Brogan AP, Widger WR, Bensadek D, Riba-Garcia I, Gaskell SJ, Kohn H. Development of a technique to determine bicyclomycin-rho binding and stoichiometry by isothermal titration calorimetry and mass spectrometry. J Am Chem Soc. 2005 Mar 02; 127(8):2741-51.
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Brogan AP, Verghese J, Widger WR, Kohn H. Bismuth-dithiol inhibition of the Escherichia coli rho transcription termination factor. J Inorg Biochem. 2005 Mar; 99(3):841-51.
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Tkach JM, Glover JR. Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J Biol Chem. 2004 Aug 20; 279(34):35692-701.
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Lum R, Tkach JM, Vierling E, Glover JR. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem. 2004 Jul 09; 279(28):29139-46.
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Weber TP, Widger WR, Kohn H. Metal-1,4-dithio-2,3-dihydroxybutane chelates: novel inhibitors of the Rho transcription termination factor. Biochemistry. 2003 Aug 05; 42(30):9121-6.
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