 Endopeptidase Clp
"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.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2006 | 1 | 0 | 1 | | 2007 | 1 | 0 | 1 | | 2008 | 1 | 0 | 1 | | 2016 | 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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Seo JH, Rivadeneira DB, Caino MC, Chae YC, Speicher DW, Tang HY, Vaira V, Bosari S, Palleschi A, Rampini P, Kossenkov AV, Languino LR, Altieri DC. The Mitochondrial Unfoldase-Peptidase Complex ClpXP Controls Bioenergetics Stress and Metastasis. PLoS Biol. 2016 07; 14(7):e1002507.
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Erbse AH, Wagner JN, Truscott KN, Spall SK, Kirstein J, Zeth K, Turgay K, Mogk A, Bukau B, Dougan DA. Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. FEBS J. 2008 Apr; 275(7):1400-1410.
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Cheng L, Naumann TA, Horswill AR, Hong SJ, Venters BJ, Tomsho JW, Benkovic SJ, Keiler KC. Discovery of antibacterial cyclic peptides that inhibit the ClpXP protease. Protein Sci. 2007 Aug; 16(8):1535-42.
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Erbse A, Schmidt R, Bornemann T, Schneider-Mergener J, Mogk A, Zahn R, Dougan DA, Bukau B. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature. 2006 Feb 09; 439(7077):753-6.
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Hinnerwisch J, Reid BG, Fenton WA, Horwich AL. Roles of the N-domains of the ClpA unfoldase in binding substrate proteins and in stable complex formation with the ClpP protease. J Biol Chem. 2005 Dec 09; 280(49):40838-44.
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Dougan DA, Reid BG, Horwich AL, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol Cell. 2002 Mar; 9(3):673-83.
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Reid BG, Fenton WA, Horwich AL, Weber-Ban EU. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc Natl Acad Sci U S A. 2001 Mar 27; 98(7):3768-72.
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Weber-Ban EU, Reid BG, Miranker AD, Horwich AL. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 1999 Sep 02; 401(6748):90-3.
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