 Holoenzymes
"Holoenzymes" 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.
Catalytically active enzymes that are formed by the combination of an apoenzyme (APOENZYMES) and its appropriate cofactors and prosthetic groups.
| Descriptor ID |
D020035
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| MeSH Number(s) |
D08.811.255
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Holoenzymes".
Below are MeSH descriptors whose meaning is more specific than "Holoenzymes".
This graph shows the total number of publications written about "Holoenzymes" by people in this website by year, and whether "Holoenzymes" 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 |
|---|
| 1998 | 0 | 1 | 1 | | 2000 | 0 | 1 | 1 | | 2001 | 0 | 2 | 2 | | 2002 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2007 | 0 | 1 | 1 | | 2010 | 0 | 2 | 2 |
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Below are the most recent publications written about "Holoenzymes" by people in Profiles.
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Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragón A. Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA. Nature. 2010 Dec 09; 468(7325):784-9.
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Widau RC, Jin Y, Dixon SA, Wadzinski BE, Gallagher PJ. Protein phosphatase 2A (PP2A) holoenzymes regulate death-associated protein kinase (DAPK) in ceramide-induced anoikis. J Biol Chem. 2010 Apr 30; 285(18):13827-38.
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Sagar GD, Gereben B, Callebaut I, Mornon JP, Zeöld A, da Silva WS, Luongo C, Dentice M, Tente SM, Freitas BC, Harney JW, Zavacki AM, Bianco AC. Ubiquitination-induced conformational change within the deiodinase dimer is a switch regulating enzyme activity. Mol Cell Biol. 2007 Jul; 27(13):4774-83.
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El-Kabbani O, Darmanin C, Schneider TR, Hazemann I, Ruiz F, Oka M, Joachimiak A, Schulze-Briese C, Tomizaki T, Mitschler A, Podjarny A. Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the binding of cyclic imide inhibitors. Proteins. 2004 Jun 01; 55(4):805-13.
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Barrera A, Fang X, Jacob J, Casey E, Thiyagarajan P, Pan T. Dimeric and monomeric Bacillus subtilis RNase P holoenzyme in the absence and presence of pre-tRNA substrates. Biochemistry. 2002 Oct 29; 41(43):12986-94.
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Loria A, Pan T. Modular construction for function of a ribonucleoprotein enzyme: the catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein. Nucleic Acids Res. 2001 May 01; 29(9):1892-7.
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Fang XW, Yang XJ, Littrell K, Niranjanakumari S, Thiyagarajan P, Fierke CA, Sosnick TR, Pan T. The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits. RNA. 2001 Feb; 7(2):233-41.
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Loria A, Pan T. The 3' substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo. RNA. 2000 Oct; 6(10):1413-22.
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Loria A, Niranjanakumari S, Fierke CA, Pan T. Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme. Biochemistry. 1998 Nov 03; 37(44):15466-73.
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