"Malates" 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.
Derivatives of malic acid (the structural formula: (COO-)2CH2CHOH), including its salts and esters.
| Descriptor ID |
D008293
|
| MeSH Number(s) |
D02.241.081.337.463 D02.241.511.505
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Malates".
Below are MeSH descriptors whose meaning is more specific than "Malates".
This graph shows the total number of publications written about "Malates" by people in this website by year, and whether "Malates" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 1996 | 1 | 0 | 1 |
| 1999 | 1 | 1 | 2 |
| 2002 | 1 | 0 | 1 |
| 2003 | 1 | 0 | 1 |
| 2007 | 0 | 1 | 1 |
| 2009 | 1 | 0 | 1 |
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Below are the most recent publications written about "Malates" by people in Profiles.
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Salmonella enterica serovar Typhimurium mutants unable to convert malate to pyruvate and oxaloacetate are avirulent and immunogenic in BALB/c mice. Infect Immun. 2009 Apr; 77(4):1397-405.
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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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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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Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD. Biochemistry. 2002 Oct 08; 41(40):12193-9.
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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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Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme. Biochemistry. 1999 Apr 06; 38(14):4398-402.
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Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Sci. 1996 Aug; 5(8):1648-54.
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Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry. 1995 Mar 14; 34(10):3253-60.
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Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate. Arch Biochem Biophys. 1992 Dec; 299(2):214-9.
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Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate. Biochemistry. 1991 Jun 11; 30(23):5764-9.