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 |
|---|---|---|
| Hyperglycinemia, Nonketotic | D020158 | 2 associated lipids |
| Liver Cirrhosis, Biliary | D008105 | 12 associated lipids |
| Nerve Degeneration | D009410 | 53 associated lipids |
| Prostatic Neoplasms | D011471 | 126 associated lipids |
| Body Weight | D001835 | 333 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 |
|---|---|---|---|---|
| Sweatt AJ et al. | Branched-chain amino acid catabolism: unique segregation of pathway enzymes in organ systems and peripheral nerves. | 2004 | Am. J. Physiol. Endocrinol. Metab. | pmid:12965870 |
| Lynch CJ et al. | Tissue-specific effects of chronic dietary leucine and norleucine supplementation on protein synthesis in rats. | 2002 | Am. J. Physiol. Endocrinol. Metab. | pmid:12217901 |
| Kiilerich K et al. | Regulation of PDH in human arm and leg muscles at rest and during intense exercise. | 2008 | Am. J. Physiol. Endocrinol. Metab. | pmid:17957032 |
| Stellingwerff T et al. | Hyperoxia decreases muscle glycogenolysis, lactate production, and lactate efflux during steady-state exercise. | 2006 | Am. J. Physiol. Endocrinol. Metab. | pmid:16403777 |
| She P et al. | Obesity-related elevations in plasma leucine are associated with alterations in enzymes involved in branched-chain amino acid metabolism. | 2007 | Am. J. Physiol. Endocrinol. Metab. | pmid:17925455 |
| Bigrigg JK et al. | Carbohydrate refeeding after a high-fat diet rapidly reverses the adaptive increase in human skeletal muscle PDH kinase activity. | 2009 | Am. J. Physiol. Regul. Integr. Comp. Physiol. | pmid:19625693 |
| Kiilerich K et al. | PGC-1alpha increases PDH content but does not change acute PDH regulation in mouse skeletal muscle. | 2010 | Am. J. Physiol. Regul. Integr. Comp. Physiol. | pmid:20720174 |
| Leblanc PJ et al. | Skeletal muscle type comparison of pyruvate dehydrogenase phosphatase activity and isoform expression: effects of obesity and endurance training. | 2008 | Am. J. Physiol. Regul. Integr. Comp. Physiol. | pmid:18716035 |
| Richards JG et al. | Glycogen phosphorylase and pyruvate dehydrogenase transformation in white muscle of trout during high-intensity exercise. | 2002 | Am. J. Physiol. Regul. Integr. Comp. Physiol. | pmid:11832404 |
| Schachter D | L-glutamine in vitro regulates rat aortic glutamate content and modulates nitric oxide formation and contractility responses. | 2007 | Am. J. Physiol., Cell Physiol. | pmid:17329397 |