MeSH term | MeSH ID | Detail |
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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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Li W et al. | Proteomic analysis of metabolic, cytoskeletal and stress response proteins in human heart failure. | 2012 | J. Cell. Mol. Med. | pmid:21545686 |
Deres P et al. | Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound. | 2005 | J. Cardiovasc. Pharmacol. | pmid:15613977 |
Raddatz G and Bisswanger H | Receptor site and stereospecifity of dihydrolipoamide dehydrogenase for R- and S-lipoamide: a molecular modeling study. | 1997 | J. Biotechnol. | pmid:9383983 |
Li M et al. | Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments. | 2006 | J. Biotechnol. | pmid:16310273 |
Chi F et al. | Identification of IbeR as a stationary-phase regulator in meningitic Escherichia coli K1 that carries a loss-of-function mutation in rpoS. | 2009 | J. Biomed. Biotechnol. | pmid:19300523 |
Matthews RG | A love affair with vitamins. | 2009 | J. Biol. Chem. | pmid:19596855 |
Picciocchi A et al. | Role of putative second transmembrane region of Nox2 protein in the structural stability and electron transfer of the phagocytic NADPH oxidase. | 2011 | J. Biol. Chem. | pmid:21659519 |
Smolle M et al. | A new level of architectural complexity in the human pyruvate dehydrogenase complex. | 2006 | J. Biol. Chem. | pmid:16679318 |
Ciszak EM et al. | How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. | 2006 | J. Biol. Chem. | pmid:16263718 |
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 |
Sauer SW et al. | Bioenergetics in glutaryl-coenzyme A dehydrogenase deficiency: a role for glutaryl-coenzyme A. | 2005 | J. Biol. Chem. | pmid:15840571 |
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 |
Rahmatullah M and Roche TE | Component requirements for NADH inhibition and spermine stimulation of pyruvate dehydrogenaseb phosphatase activity. | 1988 | J. Biol. Chem. | pmid:2836411 |
O'Connor TP et al. | 13C nuclear magnetic resonance study of the pyruvate dehydrogenase-catalyzed acetylation of dihydrolipoamide. | 1982 | J. Biol. Chem. | pmid:6801041 |
HÃ¥kansson AP and Smith AW | Enzymatic characterization of dihydrolipoamide dehydrogenase from Streptococcus pneumoniae harboring its own substrate. | 2007 | J. Biol. Chem. | pmid:17690105 |
Brautigam CA et al. | Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex. | 2009 | J. Biol. Chem. | pmid:19240034 |
Li J et al. | Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate. | 2009 | J. Biol. Chem. | pmid:19833728 |
Rajashankar KR et al. | Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis. | 2005 | J. Biol. Chem. | pmid:16093239 |
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 |
Gazaryan IG et al. | Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase. | 2002 | J. Biol. Chem. | pmid:11744691 |