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Dihydrolipoamide dehydrogenase

Dihydrolipoamide Dehydrogenase, lipoamide dehydrogenase
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, Presenilin-1, HAD, fibrillin-1
Papers on Dihydrolipoamide Dehydrogenase
Improved production of fatty acids by Saccharomyces cerevisiae through screening a cDNA library from the oleaginous yeast Yarrowia lipolytica.
Nielsen et al., Göteborg, Sweden. In Fems Yeast Res, Feb 2016
These targets include a GPI anchor protein, malate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, FA hydroxylase, farnesyltransferase, anoctamin, dihydrolipoamide dehydrogenase and phosphatidylethanolamine-binding protein.
Genetic conservation of Phosphine Resistance in the Rice Weevil Sitophilus oryzae (L.).
Ebert et al., Australia. In J Hered, Feb 2016
Each of four strongly resistant strains has an identical amino acid variant in the encoded dihydrolipoamide dehydrogenase (DLD) enzyme that was previously identified as a resistance factor in Rhyzopertha dominica and Tribolium castaneum.
Proteomics-Based Identification and Analysis of Proteins Associated with Helicobacter pylori in Gastric Cancer.
Guan et al., Guiyang, China. In Plos One, Dec 2015
We detected 135 differently expressed proteins from the three cell lines using proteome technology, and 10 differential proteins common to the three cell lines were selected and identified by LC-MS/MS as well as verified by western blot: β-actin, L-lactate dehydrogenase (LDH), dihydrolipoamide dehydrogenase (DLD), pre-mRNA-processing factor 19 homolog (PRPF19), ATP synthase, calmodulin (CaM), p64 CLCP, Ran-specific GTPase-activating protein (RanGAP), P43 and calreticulin.
Identification of DLD, by immunoproteomic analysis and evaluation as a potential vaccine antigen against three Vibrio species in Epinephelus coioides.
Jian et al., Zhanjiang, China. In Vaccine, Dec 2015
They were Outer membrane protein W (OmpW), dihydrolipoamide dehydrogenase (DLD), succinate dehydrogenase flavoprotein subunit(SDHA), elongation factor Ts(Ts), peptide ABC transporter periplasmic peptide-binding protein and phosphoenolpyruvate carboxykinase(PEPCK).
Pseudomonas aeruginosa Uses Dihydrolipoamide Dehydrogenase (Lpd) to Bind to the Human Terminal Pathway Regulators Vitronectin and Clusterin to Inhibit Terminal Pathway Complement Attack.
Zipfel et al., Jena, Germany. In Plos One, 2014
Here we identify Dihydrolipoamide dehydrogenase (Lpd), a 57 kDa moonlighting protein, as the first P. aeruginosa protein that binds the two human terminal pathway inhibitors vitronectin and clusterin.
Mitochondrial Dihydrolipoamide Dehydrogenase is Upregulated in Response to Intermittent Hypoxic Preconditioning.
Yan et al., Fort Worth, United States. In Int J Med Sci, 2014
The objective of the present study was to investigate whether mitochondrial dihydrolipoamide dehydrogenase (DLDH) would respond to IHP and if so, whether such a response could be linked to neuroprotection in ischemic stroke injury.
Pharmacological Blockade of Cannabinoid CB1 Receptors in Diet-Induced Obesity Regulates Mitochondrial Dihydrolipoamide Dehydrogenase in Muscle.
Suárez et al., Málaga, Spain. In Plos One, 2014
Dihydrolipoamide dehydrogenase (DLD), a flavoprotein component (E3) of α-ketoacid dehydrogenase complexes with diaphorase activity in mitochondria, was specifically analyzed.
Genes related to mitochondrial functions are differentially expressed in phosphine-resistant and -susceptible Tribolium castaneum.
Arthur et al., Manhattan, United States. In Bmc Genomics, 2014
Sequence polymorphism was found in transcripts encoding a known phosphine resistance gene, dihydrolipoamide dehydrogenase, in both susceptible and resistant insects.
Dihydrolipoamide Dehydrogenase Deficiency
Thoene et al., Seattle, United States. In Unknown Journal, 2014
CLINICAL CHARACTERISTICS: The phenotypes of dihydrolipoamide dehydrogenase (DLD) deficiency are an overlapping continuum that ranges from early-onset neurologic manifestations to adult-onset isolated liver involvement.
A core metabolic enzyme mediates resistance to phosphine gas.
Ebert et al., Brisbane, Australia. In Science, 2012
We find that polymorphisms responsible for genetic resistance cluster around the redox-active catalytic disulfide or the dimerization interface of dihydrolipoamide dehydrogenase (DLD) in insects (Rhyzopertha dominica and Tribolium castaneum) and nematodes (Caenorhabditis elegans).
LAPTM5 protein is a positive regulator of proinflammatory signaling pathways in macrophages.
Rotin et al., Toronto, Canada. In J Biol Chem, 2012
LAPTM5 acts as a positive modulator of inflammatory signaling pathways and hence cytokine secretion in macrophages
Thiamine and Parkinson's disease.
Nguyên et al., Westminster, United States. In J Neurol Sci, 2012
Genetic studies have helped identify a number of factors that link thiamine to PD pathology, including the DJ-1 gene, excitatory amino acid transporters (EAATs), the α-ketoglutarate dehydrogenase complex (KGDHC), coenzyme Q10 (CoQ10 or ubiquinone), lipoamide dehydrogenase (LAD), chromosome 7, transcription factor p53, the renin-angiotensin system (RAS), heme oxygenase-1 (HO-1), and poly(ADP-ribose) polymerase-1 gene (PARP-1).
Mutations in the dimer interface of dihydrolipoamide dehydrogenase promote site-specific oxidative damages in yeast and human cells.
Isaya et al., Rochester, United States. In J Biol Chem, 2011
the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations
[Role of lipoic acid in health and disease].
Goraca et al., Łódź, Poland. In Pol Merkur Lekarski, 2011
When applied systemically LA accumulates in tissues and is converted to dihyrolipoic acid (DHLA) by lipoamide dehydrogenase.
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
Chuang et al., Dallas, United States. In J Biol Chem, 2011
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
Proteins with neomorphic moonlighting functions in disease.
Jeffery, Chicago, United States. In Iubmb Life, 2011
Other changes that can result in a neomorphic moonlighting function include a mutation in SMAD4 that causes the protein to bind to new promoters and thereby alter gene transcription patterns, mutations in two isocitrate dehydrogenase isoforms that impart a new catalytic activity, and mutations in dihydrolipoamide dehydrogenase that activate a hidden protease activity.
HLA class I allelic sequence and conformation regulate leukocyte Ig-like receptor binding.
Allen et al., Cambridge, United Kingdom. In J Immunol, 2011
LILRA1 and LILRA3 generally display a greater binding preference for binding to HLA-C free heavy chain, particularly following removal of beta2-microglobulin by acid treatment.
LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence.
Gao et al., Beijing, China. In Plos One, 2010
LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2
Antioxidant properties of an endogenous thiol: Alpha-lipoic acid, useful in the prevention of cardiovascular diseases.
Rochette et al., Cluj-Napoca / Kolozsvár, Romania. In J Cardiovasc Pharmacol, 2009
ALA administered in the diet accumulates in tissues, and a substantial part is converted to DHLA via a lipoamide dehydrogenase.
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex.
Hol et al., Groningen, Netherlands. In Science, 1992
They consist of numerous copies of three different enzymes: pyruvate dehydrogenase, dihydrolipoyl transacetylase, and lipoamide dehydrogenase.
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