Dihydrolipoamide

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.

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Introduction

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.

What diseases are associated with Dihydrolipoamide?

Dihydrolipoamide is suspected in and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Dihydrolipoamide

MeSH term MeSH ID Detail
Parkinsonian Disorders D020734 20 associated lipids
Total 1

PubChem Associated disorders and diseases

What pathways are associated with Dihydrolipoamide

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Dihydrolipoamide?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with Dihydrolipoamide?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Dihydrolipoamide?

There are no associated biomedical information in the current reference collection.

What genes are associated with Dihydrolipoamide?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Dihydrolipoamide?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Dihydrolipoamide

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Authors Title Published Journal PubMed Link
Bittel C et al. The oxidant-responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)-NADP(H) reductase. 2003 FEBS Lett. pmid:14572660
Moreau R et al. Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity. 2003 Antioxid. Redox Signal. pmid:14580306
Jordan P et al. Diversity in coding tandem repeats in related Neisseria spp. 2003 BMC Microbiol. pmid:14611665
Hiromasa Y et al. Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components. 2004 J. Biol. Chem. pmid:14638692
pmid:14645106
Nordman T et al. Regeneration of the antioxidant ubiquinol by lipoamide dehydrogenase, thioredoxin reductase and glutathione reductase. 2003 Biofactors pmid:14695919
pmid:14702404
pmid:14708974
pmid:14765544
Klivenyi P et al. Mice deficient in dihydrolipoamide dehydrogenase show increased vulnerability to MPTP, malonate and 3-nitropropionic acid neurotoxicity. 2004 J. Neurochem. pmid:15009635
Fairlamb AH et al. The interaction of arsenical drugs with dihydrolipoamide and dihydrolipoamide dehydrogenase from arsenical resistant and sensitive strains of Trypanosoma brucei brucei. 1992 Mol. Biochem. Parasitol. pmid:1501642
pmid:15038962
pmid:15045077
Foster MW and Stamler JS New insights into protein S-nitrosylation. Mitochondria as a model system. 2004 J. Biol. Chem. pmid:15069080
MacDonald MJ et al. Immunochemical identification of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate and pyruvate dehydrogenase complexes partially explains the cellular toxicity of coenzyme Q0. 2004 J. Biol. Chem. pmid:15075342
pmid:15095867
pmid:15110863
Geisler DA et al. Antimycin A treatment decreases respiratory internal rotenone-insensitive NADH oxidation capacity in potato leaves. 2004 BMC Plant Biol. pmid:15140267
Rocheleau JV et al. Quantitative NAD(P)H/flavoprotein autofluorescence imaging reveals metabolic mechanisms of pancreatic islet pyruvate response. 2004 J. Biol. Chem. pmid:15148320
Kozlov G et al. Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions. 2004 BMC Biol. pmid:15161493