MeSH term | MeSH ID | Detail |
---|---|---|
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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Tam TK et al. | In situ regeneration of NADH via lipoamide dehydrogenase-catalyzed electron transfer reaction evidenced by spectroelectrochemistry. | 2012 | Bioelectrochemistry | pmid:22497727 |
pmid:22490893 | ||||
Karan R et al. | Function and biotechnology of extremophilic enzymes in low water activity. | 2012 | Aquat Biosyst | pmid:22480329 |
Sharma A et al. | Interactomic and pharmacological insights on human sirt-1. | 2012 | Front Pharmacol | pmid:22470339 |
Nam MH et al. | Comparative proteomic analysis of early salt stress-responsive proteins in roots of SnRK2 transgenic rice. | 2012 | Proteome Sci | pmid:22462395 |
ChavarrÃa M et al. | Regulatory tasks of the phosphoenolpyruvate-phosphotransferase system of Pseudomonas putida in central carbon metabolism. | 2012 | MBio | pmid:22434849 |
Jiang Y and Wang X | Comparative mitochondrial proteomics: perspective in human diseases. | 2012 | J Hematol Oncol | pmid:22424240 |
Song J and Jordan F | Interchain acetyl transfer in the E2 component of bacterial pyruvate dehydrogenase suggests a model with different roles for each chain in a trimer of the homooligomeric component. | 2012 | Biochemistry | pmid:22413895 |
pmid:22404839 | ||||
Peano C et al. | Comparative genomics and transcriptional profiles of Saccharopolyspora erythraea NRRL 2338 and a classically improved erythromycin over-producing strain. | 2012 | Microb. Cell Fact. | pmid:22401291 |