"Endopeptidase Clp" 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 ATP-dependent protease found in prokaryotes, CHLOROPLASTS, and MITOCHONDRIA. It is a soluble multisubunit complex that plays a role in the degradation of many abnormal proteins.
Descriptor ID |
D049071
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MeSH Number(s) |
D08.811.277.040.013.500.032.099.500 D08.811.277.040.025.024.032.099.500 D08.811.277.656.149.099.500 D08.811.277.656.300.065.500 D12.776.157.025.750.032.099.500 D12.776.575.374 D12.776.765.199.249
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Concept/Terms |
Endopeptidase Clp- Endopeptidase Clp
- Ti Protease
- ATP-Dependent Endoprotease Ti
- ATP Dependent Endoprotease Ti
- Endoprotease Ti, ATP-Dependent
- Protease Ti
- Clp Protease
ClpB Homolog- ClpB Homolog
- Caseinolytic Peptidase B Protein Homolog
- Mitochondrial AAA ATPase Chaperonin
- Hsp 78 Chaperone
- Chaperone, Hsp 78
ClpX Chaperone- ClpX Chaperone
- Chaperone, ClpX
- AAA(+) Chaperone ClpX
- AAA(+) Unfoldase ClpX
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Below are MeSH descriptors whose meaning is more general than "Endopeptidase Clp".
Below are MeSH descriptors whose meaning is more specific than "Endopeptidase Clp".
This graph shows the total number of publications written about "Endopeptidase Clp" by people in this website by year, and whether "Endopeptidase Clp" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2004 | 0 | 1 | 1 |
2005 | 0 | 1 | 1 |
2019 | 1 | 0 | 1 |
2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Endopeptidase Clp" by people in Profiles.
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Characterization of TR-107, a novel chemical activator of the human mitochondrial protease ClpP. Pharmacol Res Perspect. 2022 08; 10(4):e00993.
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Mitochondrial Protease ClpP is a Target for the Anticancer Compounds ONC201 and Related Analogues. ACS Chem Biol. 2019 05 17; 14(5):1020-1029.
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Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components. Proteomics. 2005 Jan; 5(1):198-211.
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The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation. J Biol Chem. 2004 Dec 03; 279(49):50886-94.