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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Brown RM et al. | Pyruvate dehydrogenase E3 binding protein (protein X) deficiency. | 2006 | Dev Med Child Neurol | pmid:16904023 |
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Smolle M et al. | A new level of architectural complexity in the human pyruvate dehydrogenase complex. | 2006 | J. Biol. Chem. | pmid:16679318 |
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Brautigam CA et al. | Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. | 2006 | Structure | pmid:16442803 |
Ciszak EM et al. | How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. | 2006 | J. Biol. Chem. | pmid:16263718 |
Boucher IW et al. | Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. | 2006 | Mol. Microbiol. | pmid:16879648 |
Kato M et al. | A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex. | 2006 | EMBO J. | pmid:17124494 |
Li M et al. | Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments. | 2006 | J. Biotechnol. | pmid:16310273 |