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 |
---|
We collected disease MeSH terms mapped to the references associated with Dihydrolipoamide
MeSH term | MeSH ID | Detail |
---|---|---|
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 |
---|
Function | Cross reference | Weighted score | Related literatures |
---|
There are no associated biomedical information in the current reference collection.
Gene | Cross reference | Weighted score | Related literatures |
---|
There are no associated biomedical information in the current reference collection.
Authors | Title | Published | Journal | PubMed Link |
---|---|---|---|---|
pmid:15178486 | ||||
pmid:15191624 | ||||
Igamberdiev AU et al. | Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide. | 2004 | FEBS Lett. | pmid:15196936 |
pmid:15250887 | ||||
Shaco-Levy R et al. | On appropriate pathology for photothermal surgery. | 2004 | Lasers Surg Med | pmid:15278925 |
pmid:15296789 | ||||
Rani K et al. | Measurement of bile acid in serum and bile with arylamine-glass-bound 3alpha-hydroxysteroid dehydrogenase and diaphorase. | 2004 | Anal. Biochem. | pmid:15301946 |
Starkov AA et al. | Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. | 2004 | J. Neurosci. | pmid:15356189 |
pmid:15389771 | ||||
Argyrou A et al. | Characterization of a new member of the flavoprotein disulfide reductase family of enzymes from Mycobacterium tuberculosis. | 2004 | J. Biol. Chem. | pmid:15456792 |
Leichert LI and Jakob U | Protein thiol modifications visualized in vivo. | 2004 | PLoS Biol. | pmid:15502869 |
pmid:15579164 | ||||
McMillan PJ et al. | The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. | 2005 | Mol. Microbiol. | pmid:15612914 |
Deres P et al. | Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound. | 2005 | J. Cardiovasc. Pharmacol. | pmid:15613977 |
Li XJ et al. | Crucial role of two potential cytosolic regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH oxidase activation. | 2005 | J. Biol. Chem. | pmid:15684431 |
Klyachko NL et al. | pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification. | 2005 | J. Biol. Chem. | pmid:15710613 |
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 |
Sauer SW et al. | Bioenergetics in glutaryl-coenzyme A dehydrogenase deficiency: a role for glutaryl-coenzyme A. | 2005 | J. Biol. Chem. | pmid:15840571 |
pmid:15878614 | ||||
Mitra K et al. | Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in spermatozoa: correlation of its localization, tyrosine phosphorylation, and activity during sperm capacitation. | 2005 | J. Biol. Chem. | pmid:15888450 |