 Proteasome Endopeptidase Complex
"Proteasome Endopeptidase Complex" 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.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
| Descriptor ID |
D046988
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| MeSH Number(s) |
D05.500.562.500 D08.811.277.656.918 D08.811.600.730
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| Concept/Terms |
Proteasome Endopeptidase Complex- Proteasome Endopeptidase Complex
- Complex, Proteasome Endopeptidase
- Endopeptidase Complex, Proteasome
- Macropain
- Macroxyproteinase
- Multicatalytic Proteinase
- Proteinase, Multicatalytic
- Prosome
- Proteasome
- 20S Proteasome
- Proteasome, 20S
- Multicatalytic Endopeptidase Complex
- Complex, Multicatalytic Endopeptidase
- Endopeptidase Complex, Multicatalytic
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Below are MeSH descriptors whose meaning is more general than "Proteasome Endopeptidase Complex".
Below are MeSH descriptors whose meaning is more specific than "Proteasome Endopeptidase Complex".
This graph shows the total number of publications written about "Proteasome Endopeptidase Complex" by people in this website by year, and whether "Proteasome Endopeptidase Complex" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 0 | 1 | 1 | | 2000 | 0 | 1 | 1 | | 2009 | 2 | 0 | 2 | | 2010 | 1 | 1 | 2 | | 2011 | 1 | 0 | 1 | | 2012 | 0 | 1 | 1 | | 2013 | 0 | 1 | 1 |
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Below are the most recent publications written about "Proteasome Endopeptidase Complex" by people in Profiles.
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Manhire-Heath R, Golenkina S, Saint R, Murray MJ. Netrin-dependent downregulation of Frazzled/DCC is required for the dissociation of the peripodial epithelium in Drosophila. Nat Commun. 2013; 4:2790.
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Tiong CT, Chen C, Zhang SJ, Li J, Soshilov A, Denison MS, Lee LS, Tam VH, Wong SP, Xu HE, Yong EL. A novel prenylflavone restricts breast cancer cell growth through AhR-mediated destabilization of ERa protein. Carcinogenesis. 2012 May; 33(5):1089-97.
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Lee KH, Minami A, Marshall RS, Book AJ, Farmer LM, Walker JM, Vierstra RD. The RPT2 subunit of the 26S proteasome directs complex assembly, histone dynamics, and gametophyte and sporophyte development in Arabidopsis. Plant Cell. 2011 Dec; 23(12):4298-317.
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Zeng X, Sigoillot F, Gaur S, Choi S, Pfaff KL, Oh DC, Hathaway N, Dimova N, Cuny GD, King RW. Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage. Cancer Cell. 2010 Oct 19; 18(4):382-95.
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Farmer LM, Book AJ, Lee KH, Lin YL, Fu H, Vierstra RD. The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis. Plant Cell. 2010 Jan; 22(1):124-42.
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Byrne A, McLaren RP, Mason P, Chai L, Dufault MR, Huang Y, Liang B, Gans JD, Zhang M, Carter K, Gladysheva TB, Teicher BA, Biemann HP, Booker M, Goldberg MA, Klinger KW, Lillie J, Madden SL, Jiang Y. Knockdown of human deubiquitinase PSMD14 induces cell cycle arrest and senescence. Exp Cell Res. 2010 Jan 15; 316(2):258-71.
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Djakovic SN, Schwarz LA, Barylko B, DeMartino GN, Patrick GN. Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II. J Biol Chem. 2009 Sep 25; 284(39):26655-65.
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Katavic V, Friesen W, Barton DL, Gossen KK, Giblin EM, Luciw T, An J, Zou J, MacKenzie SL, Keller WA, Males D, Taylor DC. Utility of the Arabidopsis FAE1 and yeast SLC1-1 genes for improvements in erucic acid and oil content in rapeseed. Biochem Soc Trans. 2000 Dec; 28(6):935-7.
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Krishnamoorthy RR, Crawford MJ, Chaturvedi MM, Jain SK, Aggarwal BB, Al-Ubaidi MR, Agarwal N. Photo-oxidative stress down-modulates the activity of nuclear factor-kappaB via involvement of caspase-1, leading to apoptosis of photoreceptor cells. J Biol Chem. 1999 Feb 05; 274(6):3734-43.
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