Lipoamide is a lipid of Fatty Acyls (FA) class. Lipoamide is associated with abnormalities such as Wiskott-Aldrich Syndrome. The involved functions are known as Phosphorylation, Protonation, Mutagenesis, Site-Directed, Oxidants and Acetylation. Lipoamide often locates in Mitochondria, Mitochondrial matrix, nucleocapsid location and Chloroplasts. The associated genes with lipoamide are Mutant Proteins, Recombinant Proteins, mycothione reductase, alanylproline and Genes, Mitochondrial.
To understand associated biological information of lipoamide, 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.
lipoamide 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 lipoamide
| MeSH term | MeSH ID | Detail |
|---|---|---|
| Body Weight | D001835 | 333 associated lipids |
| Liver Cirrhosis, Biliary | D008105 | 12 associated lipids |
| Nerve Degeneration | D009410 | 53 associated lipids |
| Prostatic Neoplasms | D011471 | 126 associated lipids |
| Hyperglycinemia, Nonketotic | D020158 | 2 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 |
|---|---|---|---|---|
| Nakai N et al. | Leucine-induced activation of translational initiation is partly regulated by the branched-chain alpha-keto acid dehydrogenase complex in C2C12 cells. | 2006 | Biochem. Biophys. Res. Commun. | pmid:16581023 |
| Shiraki M et al. | Activation of hepatic branched-chain alpha-keto acid dehydrogenase complex by tumor necrosis factor-alpha in rats. | 2005 | Biochem. Biophys. Res. Commun. | pmid:15707973 |
| Harris RA et al. | Mechanisms responsible for regulation of branched-chain amino acid catabolism. | 2004 | Biochem. Biophys. Res. Commun. | pmid:14684174 |
| Porras P et al. | Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency. | 2002 | Biochem. Biophys. Res. Commun. | pmid:12135599 |
| Spector A et al. | Thioredoxin fragment 31-36 is reduced by dihydrolipoamide and reduces oxidized protein. | 1988 | Biochem. Biophys. Res. Commun. | pmid:3122752 |
| May JM et al. | Cellular disulfide-reducing capacity: an integrated measure of cell redox capacity. | 2006 | Biochem. Biophys. Res. Commun. | pmid:16650819 |
| Kuzuya T et al. | Regulation of branched-chain amino acid catabolism in rat models for spontaneous type 2 diabetes mellitus. | 2008 | Biochem. Biophys. Res. Commun. | pmid:18541149 |
| Shilo S et al. | Selenite sensitizes mitochondrial permeability transition pore opening in vitro and in vivo: a possible mechanism for chemo-protection. | 2003 | Biochem. J. | pmid:12423204 |
| Hutson SM | The case for regulating indispensable amino acid metabolism: the branched-chain alpha-keto acid dehydrogenase kinase-knockout mouse. | 2006 | Biochem. J. | pmid:17061958 |
| Joshi MA et al. | Impaired growth and neurological abnormalities in branched-chain alpha-keto acid dehydrogenase kinase-deficient mice. | 2006 | Biochem. J. | pmid:16875466 |