"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
|
| 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
|
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 |
|---|
| 2004 | 0 | 1 | 1 |
| 2007 | 0 | 3 | 3 |
| 2014 | 0 | 1 | 1 |
| 2015 | 1 | 0 | 1 |
| 2019 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "Endopeptidase Clp" by people in Profiles.
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Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex. Nat Commun. 2021 01 12; 12(1):281.
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Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality. Cancer Cell. 2019 05 13; 35(5):721-737.e9.
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Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia. Cancer Cell. 2015 Jun 08; 27(6):864-76.
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Streptococcus pneumoniae ClpL modulates adherence to A549 human lung cells through Rap1/Rac1 activation. Infect Immun. 2014 Sep; 82(9):3802-10.
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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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Modulation of adherence, invasion, and tumor necrosis factor alpha secretion during the early stages of infection by Streptococcus pneumoniae ClpL. Infect Immun. 2007 Jun; 75(6):2996-3005.
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Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell. 2007 Jan 26; 25(2):261-71.
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M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell. 2007 Jan 26; 25(2):247-60.
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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell. 2004 Nov 24; 119(5):653-65.