MeSH term | MeSH ID | Detail |
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Parkinsonian Disorders | D020734 | 20 associated lipids |
Dihydrolipoamide is a lipid of Fatty Acyls (FA) class. Dihydrolipoamide is associated with abnormalities such as Wiskott-Aldrich Syndrome. The involved functions are known as Citric Acid Cycle, Electron Transport, NADH oxidation, Oxidation and Oxidants. Dihydrolipoamide often locates in Mitochondria, Mitochondrial matrix and Chloroplasts. The associated genes with Dihydrolipoamide are Mutant Proteins, Recombinant Proteins, mycothione reductase, Genes, Mitochondrial and alanylproline.
To understand associated biological information of Dihydrolipoamide, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
Dihydrolipoamide is suspected in and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
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We collected disease MeSH terms mapped to the references associated with Dihydrolipoamide
MeSH term | MeSH ID | Detail |
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Parkinsonian Disorders | D020734 | 20 associated lipids |
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
Location | Cross reference | Weighted score | Related literatures |
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Function | Cross reference | Weighted score | Related literatures |
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There are no associated biomedical information in the current reference collection.
Gene | Cross reference | Weighted score | Related literatures |
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There are no associated biomedical information in the current reference collection.
Authors | Title | Published | Journal | PubMed Link |
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Bunik VI et al. | Brain pyruvate and 2-oxoglutarate dehydrogenase complexes are mitochondrial targets of the CoA ester of the Refsum disease marker phytanic acid. | 2006 | FEBS Lett. | pmid:16737698 |
Lee H et al. | An integrated approach to the prediction of domain-domain interactions. | 2006 | BMC Bioinformatics | pmid:16725050 |
Mersey BD et al. | Human microRNA (miR29b) expression controls the amount of branched chain alpha-ketoacid dehydrogenase complex in a cell. | 2005 | Hum. Mol. Genet. | pmid:16203741 |
Odièvre MH et al. | A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency. | 2005 | Hum. Mutat. | pmid:15712224 |
Brautigam CA et al. | Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. | 2005 | J. Mol. Biol. | pmid:15946682 |
Sengupta J et al. | Nitric oxide in blastocyst implantation in the rhesus monkey. | 2005 | Reproduction | pmid:16123239 |
Salcedo E et al. | A glycine-cleavage complex as part of the folate one-carbon metabolism of Plasmodium falciparum. | 2005 | Trends Parasitol. | pmid:16039160 |
Da Sylva TR et al. | Somatic mutations in the mitochondria of rheumatoid arthritis synoviocytes. | 2005 | Arthritis Res. Ther. | pmid:15987486 |
Rajashankar KR et al. | Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis. | 2005 | J. Biol. Chem. | pmid:16093239 |
Tian J et al. | Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes. | 2005 | Mol. Microbiol. | pmid:16045627 |