"Ascaris suum" 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 species of parasitic nematode usually found in domestic pigs and a few other animals. Human infection can also occur, presumably as result of handling pig manure, and can lead to intestinal obstruction.
| Descriptor ID |
D017165
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| MeSH Number(s) |
B01.050.500.500.294.400.500.100.108.700
|
| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Ascaris suum".
Below are MeSH descriptors whose meaning is more specific than "Ascaris suum".
This graph shows the total number of publications written about "Ascaris suum" by people in this website by year, and whether "Ascaris suum" 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 |
|---|
| 1995 | 3 | 0 | 3 |
| 1996 | 2 | 1 | 3 |
| 1997 | 1 | 0 | 1 |
| 1999 | 1 | 2 | 3 |
| 2000 | 0 | 1 | 1 |
| 2003 | 2 | 0 | 2 |
| 2005 | 1 | 0 | 1 |
| 2006 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 2 | 0 | 2 |
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Below are the most recent publications written about "Ascaris suum" by people in Profiles.
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Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta. 2008 Dec; 1784(12):2059-64.
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Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46.
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Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88.
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Optimum activity of the phosphofructokinase from Ascaris suum requires more than one metal ion. Biochemistry. 2006 Feb 21; 45(7):2453-60.
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A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme. Biochemistry. 2005 Mar 08; 44(9):3626-35.
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Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 2003 Aug 19; 42(32):9712-21.
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Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem. 2003 Sep 26; 278(39):38051-8.
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Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60.
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Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis. Biochemistry. 1999 Aug 10; 38(32):10527-32.
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Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated. Arch Biochem Biophys. 1999 May 15; 365(2):335-43.