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anti-Human DLD Antibodies:
anti-Mouse (Murine) DLD Antibodies:
anti-Rat (Rattus) DLD Antibodies:
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Human Monoclonal DLD Primary Antibody for IHC (p), ELISA - ABIN560607
Chan, Qian, Diamond, Liu, Gritsenko, Monroe, Camp, Smith, Katze: Quantitative analysis of human immunodeficiency virus type 1-infected CD4+ cell proteome: dysregulated cell cycle progression and nuclear transport coincide with robust virus production. in Journal of virology 2007
Pig (Porcine) Polyclonal DLD Primary Antibody for IP, ELISA - ABIN4369742
Butler, Mishur, Bhaskaran, Rea: A metabolic signature for long life in the Caenorhabditis elegans Mit mutants. in Aging cell 2013
Cow (Bovine) Polyclonal DLD Primary Antibody for IHC, WB - ABIN2787688
Ayanniyi, Raji, Adegoke: Prevalence of asymptomatic sacroiliac joint dysfunction and its association with leg length discrepancies in male students in selected junior secondary schools in Ibadan. in African journal of medicine and medical sciences 2008
Show all 2 Pubmed References
These findings show that the plastidial LIPOAMIDE DEHYDROGENASE, ptLPD, isoforms are critical in vivo determinants of arsenite-mediated arsenic sensitivity in Arabidopsis and possible strategic targets for increasing arsenic tolerance. [ptLPD2]
Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase.
Lipoamide dehydrogenase significantly accelerates the conversion of a defined subset of NO donors to NO.
study found that individuals infected with HBV withwith basal core promoter (BCP (show OPN1SW Antibodies)) double mutations (A1762T, G1764A)have lower concentrations of serum DLD than those with the wild-type BCP (show OPN1SW Antibodies)
Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning.
IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer.
Case Report: novel mutation in the DLD interface giving rise to DLD deficiency.
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.
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.
the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
the E3 binding protein (show PDHX Antibodies) component of the pyruvate dehydrogenase (show PDP Antibodies) complex appear to be a rare cause of pyruvate dehydrogenase (show PDP Antibodies) deficiency
Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD (show BRCA2 Antibodies)-binding region to valine.
DLD, malic acid, and fumaric acid can be used for development of cosmeceuticals and nutraceuticals regulating the change of skin metabolism induced by the UVB overexposure.
Data show that mitochondrial diaphorases (dihydrolipoamide dehydrogenase) in the liver contribute up to 81% to the NAD(+) pool during respiratory inhibition.
Mice that are deficient in dihydrolipoamide dehydrogenase show increased vulnerability to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP (show PTPN2 Antibodies)), malonate and 3-nitropropionic acid, which have been used in models of Parkinson disease and Huntington disease (show HTT Antibodies)
identification and characterization of human and mouse D-lactate dehydrogenase (NAD) [D-LDH]
This gene encodes the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
, dihydrolipoyl dehydrogenase
, protein BfmBC
, dihydrolipoamide:NAD oxidoreductase
, glycine cleavage system L-protein
, dihydrolipoyl dehydrogenase, mitochondrial
, lipoamide dehydrogenase
, E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex
, glycine cleavage system L protein
, glycine cleavage system protein L
, lipoamide reductase
, lipoyl dehydrogenase
, branched chain alpha-keto acid dehydrogenase complex subunit E3
, dihydrolipoamide dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex)
, dihydrolipoamide: NAD+ oxidoreductase
, Dihydrolipoyl dehydrogenase, mitochondrial
, probable D-lactate dehydrogenase, mitochondrial