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 |
|---|---|---|---|---|
| Knapik-Czajka M et al. | Adverse effect of fenofibrate on branched-chain alpha-ketoacid dehydrogenase complex in rat's liver. | 2009 | Toxicology | pmid:19819289 |
| Kurakin A | The self-organizing fractal theory as a universal discovery method: the phenomenon of life. | 2011 | Theor Biol Med Model | pmid:21447162 |
| Wynn RM et al. | Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation. | 2004 | Structure | pmid:15576032 |
| Kato M et al. | Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops. | 2008 | Structure | pmid:19081061 |
| Pei XY et al. | Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multienzyme complex. | 2008 | Structure | pmid:19081062 |
| Machius M et al. | A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. | 2006 | Structure | pmid:16472748 |
| Bryk R et al. | Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. | 2002 | Science | pmid:11799204 |
| Beaudet AL | Neuroscience. Preventable forms of autism? | 2012 | Science | pmid:23087240 |
| Novarino G et al. | Mutations in BCKD-kinase lead to a potentially treatable form of autism with epilepsy. | 2012 | Science | pmid:22956686 |
| Frank RA et al. | A molecular switch and proton wire synchronize the active sites in thiamine enzymes. | 2004 | Science | pmid:15514159 |