"ATP-Dependent Proteases" 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.
Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.
| Descriptor ID |
D049069
|
| MeSH Number(s) |
D08.811.277.040.013.500.032 D08.811.277.040.025.024.032 D08.811.277.656.149 D12.776.157.025.750.032
|
| Concept/Terms |
ATP-Dependent Proteases- ATP-Dependent Proteases
- ATP Dependent Proteases
- Proteases, ATP-Dependent
- Adenosine Triphosphate-Dependent Proteolytic System
- Adenosine Triphosphate Dependent Proteolytic System
- ATP-Dependent Protease
- ATP Dependent Protease
- Protease, ATP-Dependent
- ATP-Requiring Protease
- ATP Requiring Protease
- Protease, ATP-Requiring
|
Below are MeSH descriptors whose meaning is more general than "ATP-Dependent Proteases".
Below are MeSH descriptors whose meaning is more specific than "ATP-Dependent Proteases".
This graph shows the total number of publications written about "ATP-Dependent Proteases" by people in this website by year, and whether "ATP-Dependent Proteases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1993 | 0 | 1 | 1 |
| 1996 | 0 | 2 | 2 |
| 1999 | 0 | 1 | 1 |
| 2009 | 0 | 1 | 1 |
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Below are the most recent publications written about "ATP-Dependent Proteases" by people in Profiles.
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ATP-dependent proteases differ substantially in their ability to unfold globular proteins. J Biol Chem. 2009 Jul 10; 284(28):18674-84.
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Starvation-induced Mucts62-mediated coding sequence fusion: a role for ClpXP, Lon, RpoS and Crp. Mol Microbiol. 1999 Apr; 32(2):327-43.
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Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 1996 Dec 16; 15(24):6899-909.
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Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J Mol Biol. 1996 Sep 20; 262(2):140-50.
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A role for the Clp protease in activating Mu-mediated DNA rearrangements. J Bacteriol. 1993 May; 175(9):2625-31.