DLD Antibody

1. Molecular characterization of dihydrolipoamide dehydrogenase binding sites to titanium dioxide has been reported. PMID: 28247484
2. study found that individuals infected with HBV withwith basal core promoter (BCP) double mutations (A1762T, G1764A)have lower concentrations of serum DLD than those with the wild-type BCP PMID: 27303803
3. Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning. PMID: 26078703
4. IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer. PMID: 25202086
5. Case Report: novel mutation in the DLD interface giving rise to DLD deficiency. PMID: 20652410
6. Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase. PMID: 17404228
7. This molecular dynamics study proposes the structural changes that may lead to the modulation in reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase. PMID: 24012808
8. ATP consumption is demonstrated in respiration-impaired isolated and in situ neuronal somal mitochondria from transgenic mice that exhibit a 20-48% decrease in alpha-ketoglutarate dehydrogenase activity. PMID: 23475850
9. the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations PMID: 21930696
10. Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. PMID: 21543315
11. the E3 binding protein component of the pyruvate dehydrogenase complex appear to be a rare cause of pyruvate dehydrogenase deficiency PMID: 11935326
12. Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine. PMID: 12297006
13. A c.1444A>G substitution in E3 exon 13, predictive of a p.R482G (or R447G in the processed gene product) substitution in a highly conserved domain of the protein was found. PMID: 15712224
14. Asparagine-473 residue is important for the catalytic function of dihydrolipoamide dehydrogenase. PMID: 15826505
15. the disease-causing mutations of E3 occur at three locations in the human enzyme: the dimer interface, the active site, and the FAD and NAD(+)-binding sites PMID: 15946682
16. specificity of pairing for human E3BP with E3 from its subcomplex structure to be most likely due to conformational rigidity of the binding fragment of the E3-binding domain of E3BP and its exquisite amino acid match with the E3 target interface PMID: 16263718
17. dihydrolipoamide dehydrogenase PMID: 16442803
18. The conservation of the Ile-51 residue with Ala using site-directed mutagenesis in human Dihydrolipoamide dehydrogenase(E3) was very important to the efficient catalytic function of the enzyme. PMID: 16584639
19. These results suggest that N286 and D320 play a role in the catalytic function of the E3. PMID: 17171578
20. Certain DLD mutations can simultaneously induce the loss of a primary metabolic activity and the gain of a moonlighting proteolytic activity thus contributing to the metabolic derangement associated with DLD deficiency. PMID: 17404228
21. kinetic studies suggest that T148 is not important to E3 catalytic function and R281 plays a role in the catalytic function of E3 PMID: 17960497
22. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953

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HGNC: 2898

OMIM: 238331

KEGG: hsa:1738

STRING: 9606.ENSP00000205402

UniGene: Hs.131711