"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.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 1999 | 0 | 1 | 1 |
| 2003 | 0 | 2 | 2 |
| 2009 | 0 | 2 | 2 |
| 2020 | 1 | 0 | 1 |
| 2022 | 1 | 0 | 1 |
| 2024 | 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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Compound heterozygous mutation of AFG3L2 causes autosomal recessive spinocerebellar ataxia through mitochondrial impairment and MICU1 mediated Ca2+ overload. Sci China Life Sci. 2025 Feb; 68(2):484-501.
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Inhibition of mitochondrial LonP1 protease by allosteric blockade of ATP binding and hydrolysis via CDDO and its derivatives. J Biol Chem. 2022 03; 298(3):101719.
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LONP1 de novo dominant mutation causes mitochondrial encephalopathy with loss of LONP1 chaperone activity and excessive LONP1 proteolytic activity. Mitochondrion. 2020 03; 51:68-78.
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A facile forward-genetic screen for Arabidopsis autophagy mutants reveals twenty-one loss-of-function mutations disrupting six ATG genes. Autophagy. 2019 06; 15(6):941-959.
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Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease. Am J Hum Genet. 2013 Apr 04; 92(4):605-13.
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Sampangine inhibits heme biosynthesis in both yeast and human. Eukaryot Cell. 2011 Nov; 10(11):1536-44.
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An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell. 2009 Sep 11; 35(5):574-85.
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Nuclear shape, growth and integrity in the closed mitosis of fission yeast depend on the Ran-GTPase system, the spindle pole body and the endoplasmic reticulum. J Cell Sci. 2009 Jul 15; 122(Pt 14):2464-72.
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Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol. 2003 Nov 24; 163(4):777-87.
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Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol Cell. 2003 Mar; 11(3):659-69.