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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)
Papers on Dihydrolipoamide Dehydrogenase
LAPTM5 protein is a positive regulator of proinflammatory signaling pathways in macrophages.
GeneRIF
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
Mutations in the dimer interface of dihydrolipoamide dehydrogenase promote site-specific oxidative damages in yeast and human cells.
GeneRIF
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
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
GeneRIF
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.
HLA class I allelic sequence and conformation regulate leukocyte Ig-like receptor binding.
GeneRIF
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.
GeneRIF
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
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